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Serine/threonine-protein kinase/endoribonuclease IRE1 (Endoplasmic reticulum-to-nucleus signaling 1) (Inositol-requiring protein 1) (hIRE1p) (Ire1-alpha) (IRE1a) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)]

 ERN1_HUMAN              Reviewed;         977 AA.
O75460; A1L457; A8K8N8; A8MXS7; Q59EE2;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
18-JUL-2018, entry version 183.
RecName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1 {ECO:0000305};
AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1 {ECO:0000303|PubMed:9637683};
AltName: Full=Inositol-requiring protein 1 {ECO:0000303|PubMed:9637683};
Short=hIRE1p {ECO:0000303|PubMed:9637683};
AltName: Full=Ire1-alpha {ECO:0000303|PubMed:11779464};
Short=IRE1a {ECO:0000303|PubMed:11779464};
Includes:
RecName: Full=Serine/threonine-protein kinase;
EC=2.7.11.1 {ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683};
Includes:
RecName: Full=Endoribonuclease;
EC=3.1.26.- {ECO:0000269|PubMed:21317875};
Flags: Precursor;
Name=ERN1 {ECO:0000312|HGNC:HGNC:3449};
Synonyms=IRE1 {ECO:0000312|EMBL:AAC25991.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC25991.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AUTOPHOSPHORYLATION, GLYCOSYLATION, AND MUTAGENESIS OF LYS-599.
TISSUE=Liver {ECO:0000312|EMBL:AAC25991.1};
PubMed=9637683; DOI=10.1101/gad.12.12.1812;
Tirasophon W., Welihinda A.A., Kaufman R.J.;
"A stress response pathway from the endoplasmic reticulum to the
nucleus requires a novel bifunctional protein kinase/endoribonuclease
(Ire1p) in mammalian cells.";
Genes Dev. 12:1812-1824(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Endothelial cell;
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2-977 (ISOFORM 2).
TISSUE=Brain, and Leukocyte;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=11779464; DOI=10.1016/S0092-8674(01)00611-0;
Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K.;
"XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER
stress to produce a highly active transcription factor.";
Cell 107:881-891(2001).
[8]
INTERACTION WITH TAOK3 AND TRAF2.
PubMed=11278723; DOI=10.1074/jbc.M010677200;
Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T.,
Tohyama M.;
"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.";
J. Biol. Chem. 276:13935-13940(2001).
[9] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF LYS-599.
PubMed=11175748; DOI=10.1038/35055065;
Iwawaki T., Hosoda A., Okuda T., Kamigori Y., Nomura-Furuwatari C.,
Kimata Y., Tsuru A., Kohno K.;
"Translational control by the ER transmembrane kinase/ribonuclease
IRE1 under ER stress.";
Nat. Cell Biol. 3:158-164(2001).
[10] {ECO:0000305}
FUNCTION, HOMODIMERIZATION, ENZYME REGULATION, INTERACTION WITH HSPA5,
AND MUTAGENESIS OF CYS-109; CYS-148 AND CYS-332.
PubMed=12637535; DOI=10.1074/jbc.M300418200;
Liu C.Y., Xu Z., Kaufman R.J.;
"Structure and intermolecular interactions of the luminal dimerization
domain of human IRE1alpha.";
J. Biol. Chem. 278:17680-17687(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-973, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
ADP-RIBOSYLATION BY PARP16.
PubMed=23103912; DOI=10.1038/ncb2593;
Jwa M., Chang P.;
"PARP16 is a tail-anchored endoplasmic reticulum protein required for
the PERK-and IRE1alpha-mediated unfolded protein response.";
Nat. Cell Biol. 14:1223-1230(2012).
[14]
SUBUNIT, AND INTERACTION WITH DNAJB9 AND HSPA5.
PubMed=29198525; DOI=10.1016/j.cell.2017.10.040;
Amin-Wetzel N., Saunders R.A., Kamphuis M.J., Rato C., Preissler S.,
Harding H.P., Ron D.;
"A J-Protein co-chaperone recruits bip to monomerize IRE1 and repress
the unfolded protein response.";
Cell 171:1625-1637(2017).
[15] {ECO:0000244|PDB:2HZ6}
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 24-390, SUBUNIT, AND
MUTAGENESIS OF GLN-105; ASP-123 AND TRP-125.
PubMed=16973740; DOI=10.1073/pnas.0606480103;
Zhou J., Liu C.Y., Back S.H., Clark R.L., Peisach D., Xu Z.,
Kaufman R.J.;
"The crystal structure of human IRE1 luminal domain reveals a
conserved dimerization interface required for activation of the
unfolded protein response.";
Proc. Natl. Acad. Sci. U.S.A. 103:14343-14348(2006).
[16] {ECO:0000244|PDB:3P23}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 547-977 IN COMPLEX WITH ADP,
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION,
AND COFACTOR.
PubMed=21317875; DOI=10.1038/emboj.2011.18;
Ali M.M., Bagratuni T., Davenport E.L., Nowak P.R.,
Silva-Santisteban M.C., Hardcastle A., McAndrews C., Rowlands M.G.,
Morgan G.J., Aherne W., Collins I., Davies F.E., Pearl L.H.;
"Structure of the Ire1 autophosphorylation complex and implications
for the unfolded protein response.";
EMBO J. 30:894-905(2011).
[17]
VARIANTS [LARGE SCALE ANALYSIS] SER-244; MET-418; ARG-474; TRP-635;
SER-700; PHE-769 AND LEU-830.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[18]
FUNCTION, INTERACTION WITH PDIA6, SUBUNIT, AND MUTAGENESIS OF CYS-148.
PubMed=24508390; DOI=10.1016/j.molcel.2014.01.004;
Eletto D., Eletto D., Dersh D., Gidalevitz T., Argon Y.;
"Protein disulfide isomerase A6 controls the decay of IRE1alpha
signaling via disulfide-dependent association.";
Mol. Cell 53:562-576(2014).
-!- FUNCTION: Serine/threonine-protein kinase and endoribonuclease
that acts as a key sensor for the endoplasmic reticulum unfolded
protein response (UPR) (PubMed:11779464, PubMed:11175748,
PubMed:12637535, PubMed:9637683, PubMed:21317875). In unstressed
cells, the endoplasmic reticulum luminal domain is maintained in
its inactive monomeric state by binding to the endoplasmic
reticulum chaperone HSPA5/BiP (PubMed:21317875). Accumulation of
misfolded protein in the endoplasmic reticulum causes release of
HSPA5/BiP, allowing the luminal domain to homodimerize, promoting
autophosphorylation of the kinase domain and subsequent activation
of the endoribonuclease activity (PubMed:21317875). The
endoribonuclease activity is specific for XBP1 mRNA and excises 26
nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:24508390,
PubMed:21317875). The resulting spliced transcript of XBP1 encodes
a transcriptional activator protein that up-regulates expression
of UPR target genes (PubMed:11779464, PubMed:24508390,
PubMed:21317875). {ECO:0000269|PubMed:11175748,
ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:12637535,
ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683,
ECO:0000305|PubMed:24508390}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:21317875,
ECO:0000269|PubMed:9637683};
-!- ENZYME REGULATION: The kinase domain is activated by trans-
autophosphorylation following homodimerization (PubMed:12637535,
PubMed:9637683). Kinase activity is required for activation of the
endoribonuclease domain (PubMed:12637535, PubMed:9637683).
Endoribonuclease activity is specifically inhibited by hydroxy-
aryl-aldehydes (HAA) (By similarity).
{ECO:0000250|UniProtKB:Q9EQY0, ECO:0000269|PubMed:12637535,
ECO:0000269|PubMed:9637683}.
-!- SUBUNIT: Monomer (PubMed:29198525, PubMed:16973740). Homodimer;
disulfide-linked; homodimerization takes place in response to
endoplasmic reticulum stress and promotes activation of the kinase
and endoribonuclease activities (PubMed:12637535, PubMed:24508390,
PubMed:16973740, PubMed:21317875). Dimer formation is driven by
hydrophobic interactions within the N-terminal luminal domains and
stabilized by disulfide bridges (PubMed:12637535). Interacts (via
the luminal region) with DNAJB9/ERdj4; interaction takes place in
unstressed cells and promotes recruitment of HSPA5/BiP
(PubMed:29198525). Interacts (via the luminal region) with
HSPA5/BiP; HSPA5/BiP is a negative regulator of the unfolded
protein response (UPR) that prevents homodimerization of ERN1/IRE1
and subsequent activation of the protein (PubMed:12637535,
PubMed:29198525). Interacts with PDIA6, a negative regulator of
the UPR; the interaction is direct and disrupts homodimerization
(PubMed:24508390). Interacts with DAB2IP (via PH domain); the
interaction occurs in a endoplasmic reticulum stress-induced
dependent manner and is required for subsequent recruitment of
TRAF2 to ERN1/IRE1 (By similarity). Interacts with TAOK3 and TRAF2
(PubMed:11278723). {ECO:0000250|UniProtKB:Q9EQY0,
ECO:0000269|PubMed:11278723, ECO:0000269|PubMed:12637535,
ECO:0000269|PubMed:16973740, ECO:0000269|PubMed:24508390,
ECO:0000269|PubMed:29198525}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-371750, EBI-371750;
O08734:Bak1 (xeno); NbExp=2; IntAct=EBI-371750, EBI-822441;
Q07812:BAX; NbExp=2; IntAct=EBI-371750, EBI-516580;
Q07813:Bax (xeno); NbExp=2; IntAct=EBI-371750, EBI-700711;
P0DMV8:HSPA1A; NbExp=5; IntAct=EBI-15600828, EBI-11820565;
P11021:HSPA5; NbExp=4; IntAct=EBI-15600828, EBI-354921;
P20029:Hspa5 (xeno); NbExp=2; IntAct=EBI-371750, EBI-772325;
Q13438:OS9; NbExp=2; IntAct=EBI-15600828, EBI-725454;
Q9UBV2:SEL1L; NbExp=2; IntAct=EBI-15600828, EBI-358766;
Q86TM6:SYVN1; NbExp=3; IntAct=EBI-15600828, EBI-947849;
Q9H2K8:TAOK3; NbExp=3; IntAct=EBI-371750, EBI-1384100;
Q12933:TRAF2; NbExp=3; IntAct=EBI-371750, EBI-355744;
Q969M3:YIPF5; NbExp=3; IntAct=EBI-371750, EBI-2124787;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:9637683}; Single-pass type I membrane protein
{ECO:0000269|PubMed:9637683}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75460-1; Sequence=Displayed;
Name=2;
IsoId=O75460-2; Sequence=VSP_034582, VSP_034583;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. High levels observed
in pancreatic tissue. {ECO:0000269|PubMed:9637683}.
-!- PTM: Autophosphorylated following homodimerization.
Autophosphorylation promotes activation of the endoribonuclease
domain. {ECO:0000269|PubMed:12637535, ECO:0000269|PubMed:21317875,
ECO:0000269|PubMed:9637683}.
-!- PTM: ADP-ribosylated by PARP16 upon ER stress, which increases
both kinase and endonuclease activities.
{ECO:0000269|PubMed:23103912}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; AF059198; AAC25991.1; -; mRNA.
EMBL; AK292403; BAF85092.1; -; mRNA.
EMBL; DA254477; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB209869; BAD93106.1; -; mRNA.
EMBL; AC005803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94214.1; -; Genomic_DNA.
EMBL; BC130405; AAI30406.1; -; mRNA.
EMBL; BC130407; AAI30408.1; -; mRNA.
EMBL; BI912495; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS45762.1; -. [O75460-1]
RefSeq; NP_001424.3; NM_001433.3. [O75460-1]
UniGene; Hs.133982; -.
UniGene; Hs.700027; -.
UniGene; Hs.744953; -.
PDB; 2HZ6; X-ray; 3.10 A; A=24-390.
PDB; 3P23; X-ray; 2.70 A; A/B/C/D=547-977.
PDB; 4U6R; X-ray; 2.50 A; A=547-977.
PDB; 4YZ9; X-ray; 2.46 A; A/B/C=562-966.
PDB; 4YZC; X-ray; 2.49 A; A/B=562-966.
PDB; 4YZD; X-ray; 3.10 A; A/B/C=562-966.
PDB; 4Z7G; X-ray; 2.60 A; A/B=562-977.
PDB; 4Z7H; X-ray; 2.90 A; A/B=562-977.
PDB; 5HGI; X-ray; 2.58 A; A=547-977.
PDBsum; 2HZ6; -.
PDBsum; 3P23; -.
PDBsum; 4U6R; -.
PDBsum; 4YZ9; -.
PDBsum; 4YZC; -.
PDBsum; 4YZD; -.
PDBsum; 4Z7G; -.
PDBsum; 4Z7H; -.
PDBsum; 5HGI; -.
ProteinModelPortal; O75460; -.
SMR; O75460; -.
BioGrid; 108391; 33.
DIP; DIP-31711N; -.
IntAct; O75460; 22.
MINT; O75460; -.
STRING; 9606.ENSP00000401445; -.
BindingDB; O75460; -.
ChEMBL; CHEMBL1163101; -.
GuidetoPHARMACOLOGY; 2020; -.
iPTMnet; O75460; -.
PhosphoSitePlus; O75460; -.
BioMuta; ERN1; -.
EPD; O75460; -.
MaxQB; O75460; -.
PaxDb; O75460; -.
PeptideAtlas; O75460; -.
PRIDE; O75460; -.
ProteomicsDB; 50021; -.
ProteomicsDB; 50022; -. [O75460-2]
DNASU; 2081; -.
Ensembl; ENST00000433197; ENSP00000401445; ENSG00000178607. [O75460-1]
Ensembl; ENST00000606895; ENSP00000475519; ENSG00000178607. [O75460-2]
GeneID; 2081; -.
KEGG; hsa:2081; -.
UCSC; uc002jdz.3; human. [O75460-1]
CTD; 2081; -.
DisGeNET; 2081; -.
EuPathDB; HostDB:ENSG00000178607.15; -.
GeneCards; ERN1; -.
H-InvDB; HIX0014084; -.
HGNC; HGNC:3449; ERN1.
HPA; CAB009495; -.
HPA; HPA027730; -.
MIM; 604033; gene.
neXtProt; NX_O75460; -.
OpenTargets; ENSG00000178607; -.
PharmGKB; PA27861; -.
eggNOG; KOG1027; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00390000015684; -.
HOGENOM; HOG000012929; -.
HOVERGEN; HBG051506; -.
InParanoid; O75460; -.
KO; K08852; -.
OMA; MDWRENI; -.
OrthoDB; EOG091G049V; -.
PhylomeDB; O75460; -.
TreeFam; TF313986; -.
Reactome; R-HSA-381070; IRE1alpha activates chaperones.
SignaLink; O75460; -.
SIGNOR; O75460; -.
ChiTaRS; ERN1; human.
EvolutionaryTrace; O75460; -.
GeneWiki; ERN1; -.
GenomeRNAi; 2081; -.
PRO; PR:O75460; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000178607; -.
CleanEx; HS_ERN1; -.
Genevisible; O75460; HS.
GO; GO:1990597; C:AIP1-IRE1 complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:1990332; C:Ire1 complex; NAS:ParkinsonsUK-UCL.
GO; GO:1990630; C:IRE1-RACK1-PP2A complex; IDA:ParkinsonsUK-UCL.
GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; IDA:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051879; F:Hsp90 protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:ParkinsonsUK-UCL.
GO; GO:0034620; P:cellular response to unfolded protein; IDA:ParkinsonsUK-UCL.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
GO; GO:1901142; P:insulin metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; IDA:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0006379; P:mRNA cleavage; ISS:UniProtKB.
GO; GO:0098787; P:mRNA cleavage involved in mRNA processing; IDA:ParkinsonsUK-UCL.
GO; GO:0070054; P:mRNA splicing, via endonucleolytic cleavage and ligation; IDA:UniProtKB.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:1990579; P:peptidyl-serine trans-autophosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
GO; GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1440.180; -; 1.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR010513; KEN_dom.
InterPro; IPR038357; KEN_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR018391; PQQ_beta_propeller_repeat.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR018997; PUB_domain.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF00069; Pkinase; 1.
Pfam; PF06479; Ribonuc_2-5A; 1.
SMART; SM00564; PQQ; 5.
SMART; SM00580; PUG; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50998; SSF50998; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51392; KEN; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing; Apoptosis;
ATP-binding; Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Hydrolase; Kinase; Magnesium; Membrane; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Signal; Transcription; Transcription regulation; Transferase;
Transmembrane; Transmembrane helix; Unfolded protein response.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 977 Serine/threonine-protein
kinase/endoribonuclease IRE1.
/FTId=PRO_0000024327.
TOPO_DOM 19 443 Lumenal. {ECO:0000255}.
TRANSMEM 444 464 Helical. {ECO:0000255}.
TOPO_DOM 465 977 Cytoplasmic. {ECO:0000255}.
DOMAIN 571 832 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 835 963 KEN. {ECO:0000255|PROSITE-
ProRule:PRU00725}.
NP_BIND 577 585 ATP. {ECO:0000250|UniProtKB:P32361,
ECO:0000255|PROSITE-ProRule:PRU00159}.
NP_BIND 643 645 ATP. {ECO:0000244|PDB:3P23,
ECO:0000269|PubMed:21317875}.
NP_BIND 690 693 ATP. {ECO:0000244|PDB:3P23,
ECO:0000269|PubMed:21317875}.
REGION 906 907 Hydroxy-aryl-aldehyde inhibitor binding.
{ECO:0000250|UniProtKB:Q9EQY0}.
ACT_SITE 688 688 Proton acceptor.
{ECO:0000250|UniProtKB:P32361,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 599 599 ATP. {ECO:0000244|PDB:3P23,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:21317875,
ECO:0000269|PubMed:9637683}.
BINDING 711 711 ATP. {ECO:0000244|PDB:3P23,
ECO:0000269|PubMed:21317875}.
BINDING 892 892 Hydroxy-aryl-aldehyde inhibitor.
{ECO:0000250|UniProtKB:Q9EQY0}.
MOD_RES 973 973 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 19 70 IFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKED
PVLQVPTHVEE -> VSDRGAWGGGQLATAGSGPGQRRGAG
AGVRAGSATAAARCPVSPAVGGSGRA (in isoform
2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_034582.
VAR_SEQ 71 977 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_034583.
VARIANT 244 244 N -> S (in a renal clear cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040488.
VARIANT 418 418 V -> M (in dbSNP:rs55869215).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040489.
VARIANT 474 474 L -> R (in a lung adenocarcinoma sample;
somatic mutation; dbSNP:rs186305118).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040490.
VARIANT 635 635 R -> W (in a gastric adenocarcinoma
sample; somatic mutation;
dbSNP:rs146710304).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040491.
VARIANT 700 700 N -> S (in dbSNP:rs918253870).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040492.
VARIANT 769 769 S -> F (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040493.
VARIANT 830 830 P -> L (in an ovarian serous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040494.
MUTAGEN 105 105 Q->E: Impaired ability to homodimerize.
{ECO:0000269|PubMed:16973740}.
MUTAGEN 109 109 C->S: No effect on dimerization.
{ECO:0000269|PubMed:12637535}.
MUTAGEN 123 123 D->P: Abolishes ability to homodimerize.
{ECO:0000269|PubMed:16973740}.
MUTAGEN 125 125 W->A: Abolishes ability to homodimerize.
{ECO:0000269|PubMed:16973740}.
MUTAGEN 148 148 C->S: No effect on dimerization. Weakens
dimer; when associated with S-332.
Abolishes interaction with PDIA6.
Prolonged splicing of XBP1, probably due
to prolonged activation of PDIA6.
Inhibits formation of oxidized multimeric
forms of ERN1 in response to ER stress.
{ECO:0000269|PubMed:12637535,
ECO:0000269|PubMed:24508390}.
MUTAGEN 332 332 C->S: No effect on dimerization. Weakens
dimer; when associated with S-148.
{ECO:0000269|PubMed:12637535}.
MUTAGEN 599 599 K->A: Loss of autophosphorylation and of
endoribonuclease activity. Inhibition of
growth arrest.
{ECO:0000269|PubMed:11175748,
ECO:0000269|PubMed:9637683}.
CONFLICT 190 191 DV -> EG (in Ref. 1; AAC25991).
{ECO:0000305}.
CONFLICT 768 768 I -> V (in Ref. 1; AAC25991).
{ECO:0000305}.
CONFLICT 816 816 D -> G (in Ref. 2; BAF85092).
{ECO:0000305}.
CONFLICT 824 825 KH -> ND (in Ref. 1; AAC25991).
{ECO:0000305}.
CONFLICT 880 880 V -> D (in Ref. 1; AAC25991).
{ECO:0000305}.
CONFLICT 904 904 M -> T (in Ref. 2; BAF85092).
{ECO:0000305}.
CONFLICT 924 924 S -> T (in Ref. 1; AAC25991).
{ECO:0000305}.
STRAND 32 37 {ECO:0000244|PDB:2HZ6}.
STRAND 40 46 {ECO:0000244|PDB:2HZ6}.
TURN 47 49 {ECO:0000244|PDB:2HZ6}.
STRAND 52 57 {ECO:0000244|PDB:2HZ6}.
STRAND 73 75 {ECO:0000244|PDB:2HZ6}.
TURN 77 79 {ECO:0000244|PDB:2HZ6}.
STRAND 82 84 {ECO:0000244|PDB:2HZ6}.
STRAND 93 95 {ECO:0000244|PDB:2HZ6}.
HELIX 100 104 {ECO:0000244|PDB:2HZ6}.
STRAND 120 128 {ECO:0000244|PDB:2HZ6}.
STRAND 154 164 {ECO:0000244|PDB:2HZ6}.
STRAND 168 172 {ECO:0000244|PDB:2HZ6}.
STRAND 176 182 {ECO:0000244|PDB:2HZ6}.
STRAND 197 201 {ECO:0000244|PDB:2HZ6}.
STRAND 205 209 {ECO:0000244|PDB:2HZ6}.
TURN 211 213 {ECO:0000244|PDB:2HZ6}.
STRAND 216 221 {ECO:0000244|PDB:2HZ6}.
STRAND 226 231 {ECO:0000244|PDB:2HZ6}.
STRAND 238 240 {ECO:0000244|PDB:2HZ6}.
STRAND 243 246 {ECO:0000244|PDB:2HZ6}.
HELIX 247 264 {ECO:0000244|PDB:2HZ6}.
HELIX 273 279 {ECO:0000244|PDB:2HZ6}.
STRAND 280 284 {ECO:0000244|PDB:2HZ6}.
STRAND 286 288 {ECO:0000244|PDB:2HZ6}.
STRAND 297 300 {ECO:0000244|PDB:2HZ6}.
TURN 359 361 {ECO:0000244|PDB:2HZ6}.
STRAND 564 566 {ECO:0000244|PDB:4YZC}.
STRAND 567 580 {ECO:0000244|PDB:4YZ9}.
TURN 581 583 {ECO:0000244|PDB:4YZ9}.
STRAND 584 591 {ECO:0000244|PDB:4YZ9}.
STRAND 594 601 {ECO:0000244|PDB:4YZ9}.
HELIX 603 605 {ECO:0000244|PDB:4YZ9}.
HELIX 606 617 {ECO:0000244|PDB:4YZ9}.
STRAND 628 633 {ECO:0000244|PDB:4YZ9}.
STRAND 638 642 {ECO:0000244|PDB:4YZ9}.
STRAND 645 648 {ECO:0000244|PDB:4YZ9}.
HELIX 649 655 {ECO:0000244|PDB:4YZ9}.
HELIX 657 661 {ECO:0000244|PDB:4YZ9}.
HELIX 665 681 {ECO:0000244|PDB:4YZ9}.
TURN 691 693 {ECO:0000244|PDB:4YZ9}.
STRAND 694 697 {ECO:0000244|PDB:4YZ9}.
TURN 701 703 {ECO:0000244|PDB:4YZD}.
STRAND 707 709 {ECO:0000244|PDB:4YZ9}.
HELIX 712 714 {ECO:0000244|PDB:4YZC}.
HELIX 740 743 {ECO:0000244|PDB:4YZC}.
HELIX 754 768 {ECO:0000244|PDB:4YZ9}.
HELIX 778 780 {ECO:0000244|PDB:4YZ9}.
HELIX 781 787 {ECO:0000244|PDB:4YZ9}.
STRAND 793 795 {ECO:0000244|PDB:4YZC}.
HELIX 800 812 {ECO:0000244|PDB:4YZ9}.
HELIX 817 819 {ECO:0000244|PDB:4YZ9}.
HELIX 823 827 {ECO:0000244|PDB:4YZ9}.
HELIX 830 832 {ECO:0000244|PDB:4YZ9}.
HELIX 835 849 {ECO:0000244|PDB:4YZ9}.
STRAND 854 856 {ECO:0000244|PDB:4YZ9}.
HELIX 857 865 {ECO:0000244|PDB:4YZ9}.
HELIX 867 870 {ECO:0000244|PDB:4YZ9}.
STRAND 874 878 {ECO:0000244|PDB:4YZ9}.
HELIX 880 887 {ECO:0000244|PDB:4YZ9}.
STRAND 888 890 {ECO:0000244|PDB:4YZ9}.
HELIX 897 909 {ECO:0000244|PDB:4YZ9}.
HELIX 911 913 {ECO:0000244|PDB:4YZ9}.
HELIX 916 922 {ECO:0000244|PDB:4YZ9}.
HELIX 927 936 {ECO:0000244|PDB:4YZ9}.
HELIX 940 947 {ECO:0000244|PDB:4YZ9}.
HELIX 948 951 {ECO:0000244|PDB:4YZ9}.
STRAND 952 954 {ECO:0000244|PDB:3P23}.
HELIX 955 957 {ECO:0000244|PDB:4YZ9}.
TURN 958 960 {ECO:0000244|PDB:4YZ9}.
SEQUENCE 977 AA; 109735 MW; A2DF808CCE015536 CRC64;
MPARRLLLLL TLLLPGLGIF GSTSTVTLPE TLLFVSTLDG SLHAVSKRTG SIKWTLKEDP
VLQVPTHVEE PAFLPDPNDG SLYTLGSKNN EGLTKLPFTI PELVQASPCR SSDGILYMGK
KQDIWYVIDL LTGEKQQTLS SAFADSLCPS TSLLYLGRTE YTITMYDTKT RELRWNATYF
DYAASLPEDD VDYKMSHFVS NGDGLVVTVD SESGDVLWIQ NYASPVVAFY VWQREGLRKV
MHINVAVETL RYLTFMSGEV GRITKWKYPF PKETEAKSKL TPTLYVGKYS TSLYASPSMV
HEGVAVVPRG STLPLLEGPQ TDGVTIGDKG ECVITPSTDV KFDPGLKSKN KLNYLRNYWL
LIGHHETPLS ASTKMLERFP NNLPKHRENV IPADSEKKSF EEVINLVDQT SENAPTTVSR
DVEEKPAHAP ARPEAPVDSM LKDMATIILS TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ
KELEKIQLLQ QQQQQLPFHP PGDTAQDGEL LDTSGPYSES SGTSSPSTSP RASNHSLCSG
SSASKAGSSP SLEQDDGDEE TSVVIVGKIS FCPKDVLGHG AEGTIVYRGM FDNRDVAVKR
ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ EYVEQKDFAH
LGLEPITLLQ QTTSGLAHLH SLNIVHRDLK PHNILISMPN AHGKIKAMIS DFGLCKKLAV
GRHSFSRRSG VPGTEGWIAP EMLSEDCKEN PTYTVDIFSA GCVFYYVISE GSHPFGKSLQ
RQANILLGAC SLDCLHPEKH EDVIARELIE KMIAMDPQKR PSAKHVLKHP FFWSLEKQLQ
FFQDVSDRIE KESLDGPIVK QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL
LRAMRNKKHH YRELPAEVRE TLGSLPDDFV CYFTSRFPHL LAHTYRAMEL CSHERLFQPY
YFHEPPEPQP PVTPDAL


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