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Q9Z2E3 (ERN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase/endoribonuclease IRE2
Alternative name(s):
Endoplasmic reticulum-to-nucleus signaling 2
Inositol-requiring protein 2
Ire1-beta
Short name=IRE1b
Short name=mIre1

Including the following 2 domains:

  1. Serine/threonine-protein kinase
    EC=2.7.11.1
  2. Endoribonuclease
    EC=3.1.26.-
Gene names
Name:Ern2
Synonyms:Ire2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Role in expression of the DDIT3 transcription factor, required for the unfolded-protein response, growth arrest and apoptosis. Has no effect on 28S ribosomal RNA cleavage, unlike the corresponding human protein. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB O75460

Cofactor

Magnesium By similarity. UniProtKB O75460

Enzyme regulation

The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain By similarity. UniProtKB O75460

Subcellular location

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

Post-translational modification

Autophosphorylated By similarity. UniProtKB O75460

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
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
Kinase
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle arrest

Inferred from direct assay Ref.1. Source: UniProtKB

induction of apoptosis

Inferred from direct assay Ref.1. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: InterPro

negative regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: Compara

rRNA catabolic process

Inferred from electronic annotation. Source: Compara

regulation of transcription, DNA-dependent

Inferred from direct assay Ref.1. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

endonuclease activity

Inferred from electronic annotation. Source: Compara

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ribonuclease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 911878Serine/threonine-protein kinase/endoribonuclease IRE2
PRO_0000024330

Regions

Topological domain35 – 426392Lumenal Potential
Transmembrane427 – 44721Helical; Potential
Topological domain448 – 911464Cytoplasmic Potential
Domain508 – 768261Protein kinase
Domain771 – 899129KEN
Nucleotide binding514 – 5229ATP By similarity UniProtKB P32361

Sites

Active site6251Proton acceptor By similarity UniProtKB P32361
Binding site5361ATP By similarity UniProtKB O75460

Amino acid modifications

Glycosylation1781N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict451L → W in AAC64400. Ref.1
Sequence conflict951Q → H in AAC64400. Ref.1
Sequence conflict971Q → L in AAC64400. Ref.1
Sequence conflict6891S → N in AAC64400. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z2E3 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 77E210F1D8D15737

FASTA911101,262
        10         20         30         40         50         60 
MARPVQRFQL WSPLGFLLQL VTLLGKLGPQ VQSVRPESLL FVSTLDGSLH ALNKQTGDLK 

        70         80         90        100        110        120 
WTVKDDPIIQ GPMYVTEMAF LSDPADGSLY VLGTQKQQGL MKLPFTIPEL VHASPCRSSD 

       130        140        150        160        170        180 
GVFYTGRKQD AWFVVDPESG ETQMTLTTEG LSTPQLFIGR TQYTVSMHDL RTPALRWNTT 

       190        200        210        220        230        240 
YRRYSAPLLN GSPGKYMSHL TSCGMGLLLT VDPGSGIVLW TQDLGVPVTG IYTWHQDGLH 

       250        260        270        280        290        300 
QLPHLTLARD TLHFLVLRWG HIRLPASSYQ DTATQFSSLD TQLLMTLYVG KEEAGFYVSK 

       310        320        330        340        350        360 
ALVHAGVALV PRGLTLAPMD GPTTDEVTLQ VSGEREGSPS TAVRYPSGSV ALPSQWLLIG 

       370        380        390        400        410        420 
YHEPPPVLHT TMLRVHPIPG KVSAETRASE DLHAPPVFFE LLNLRREDPE LHPEEKASDS 

       430        440        450        460        470        480 
YPGLGSQDLL AATFTAILLG AWVLYLMRQQ QQSPSAPAGP PDLSQDAQGQ LSRDILQDQR 

       490        500        510        520        530        540 
RFQSPSEPAQ PPHDPEAGQP TVVGKISFNP KDVLGRGAGG TFVFRGQFEG RAVAVKRLLR 

       550        560        570        580        590        600 
ECFGLVRREV QLLQESDRHP NVLRYFCTEH GPQFHYIALE LCQASLQEYV ESPDLDRWGL 

       610        620        630        640        650        660 
EPTTVLQQMM SGLAHLHSLH IVHRDLKPAN ILMAGPDSQG QGRVVISDFG LCKKLPVGRC 

       670        680        690        700        710        720 
SFSLHSGIPG TEGWMAPELL QLPPDSPTSA VDIFSAGCVF YYVLSGGSHP FGESLYRQAN 

       730        740        750        760        770        780 
ILSGDPCLAQ LQEETHDKVV ALDLVRAMLS LLPQDRPSAG WVLAHPLFWS RAKELQFFQD 

       790        800        810        820        830        840 
VSDWLEKEPD QGPLVSALEA GSYKVVREDW HKHISAPLQA DLKRFRSYKG TSVRDLLRAM 

       850        860        870        880        890        900 
RNKKHHYREL PAEVRQTLGQ LPAGFIQYFT QRFPRLLLHT HRAMRTCASE SLFLPYYPPA 

       910 
LEARRPDATK S

« Hide

References

« Hide 'large scale' references
[1]"Cloning of mammalian Ire1 reveals a diversity in the ER stress responses."
Wang X.-Z., Harding H.P., Zhang Y., Jolicoeur E.M., Kuroda M., Ron D.
EMBO J. 17:5708-5717(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Thymus.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF071777 mRNA. Translation: AAC64400.1.
AK153659 mRNA. Translation: BAE32136.1.
CH466531 Genomic DNA. Translation: EDL17275.1.
IPIIPI00323626.
RefSeqNP_036146.2. NM_012016.2.
UniGeneMm.20452.

3D structure databases

ProteinModelPortalQ9Z2E3.
SMRQ9Z2E3. Positions 36-310, 472-897.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033153.

PTM databases

PhosphoSiteQ9Z2E3.

Proteomic databases

PRIDEQ9Z2E3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033153; ENSMUSP00000033153; ENSMUSG00000030866.
GeneID26918.
KEGGmmu:26918.
UCSCuc009joq.1. mouse.

Organism-specific databases

CTD10595.
MGIMGI:1349436. Ern2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00390000015684.
HOGENOMHOG000012929.
HOVERGENHBG051506.
InParanoidQ3U5E3.
KOK11715.
OMAMLRVHPT.
OrthoDBEOG4894M4.

Gene expression databases

ArrayExpressQ9Z2E3.
BgeeQ9Z2E3.
GenevestigatorQ9Z2E3.
GermOnlineENSMUSG00000030866. Mus musculus.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
InterProIPR010513. KEN_dom.
IPR011009. Kinase-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR002372. PQQ_repeat.
IPR000719. Prot_kinase_cat_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.
PF01011. PQQ. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
SMARTSM00564. PQQ. 4 hits.
SM00580. PUG. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
SSF50998. Quin_alc_DH_like. 1 hit.
PROSITEPS51392. KEN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304797.
SOURCESearch...

Entry information

Entry nameERN2_MOUSE
AccessionPrimary (citable) accession number: Q9Z2E3
Secondary accession number(s): Q3U5E3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents