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Serine/threonine-protein kinase SMG1 (SMG-1) (hSMG-1) (EC 2.7.11.1) (61E3.4) (Lambda/iota protein kinase C-interacting protein) (Lambda-interacting protein)

 SMG1_HUMAN              Reviewed;        3661 AA.
Q96Q15; O43305; Q13284; Q8NFX2; Q96QV0; Q96RW3;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
22-NOV-2017, entry version 149.
RecName: Full=Serine/threonine-protein kinase SMG1;
Short=SMG-1;
Short=hSMG-1;
EC=2.7.11.1;
AltName: Full=61E3.4;
AltName: Full=Lambda/iota protein kinase C-interacting protein;
Short=Lambda-interacting protein;
Name=SMG1; Synonyms=ATX, KIAA0421, LIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=9566925; DOI=10.1128/MCB.18.5.3069;
Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.;
"Localization of atypical protein kinase C isoforms into lysosome-
targeted endosomes through interaction with p62.";
Mol. Cell. Biol. 18:3069-3080(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION OF
RENT1, ALTERNATIVE SPLICING, ENZYME REGULATION, PHOSPHORYLATION,
INTERACTION WITH RENT1; UPF2 AND UPF3, AND MUTAGENESIS OF ASP-2335.
PubMed=11544179; DOI=10.1101/gad.913001;
Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S.;
"Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein
kinase, associates with components of the mRNA surveillance complex
and is involved in the regulation of nonsense-mediated mRNA decay.";
Genes Dev. 15:2215-2228(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PHOSPHORYLATION OF
RENT1, COFACTOR, ENZYME REGULATION, AND MUTAGENESIS OF ASP-2335.
PubMed=11331269; DOI=10.1074/jbc.C100144200;
Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P.;
"Cloning of a novel phosphatidylinositol kinase-related kinase:
characterization of the human SMG-1 RNA surveillance protein.";
J. Biol. Chem. 276:22709-22714(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION OF
TP53, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION,
MUTAGENESIS OF ASP-2335, AND VARIANTS CYS-144 AND LYS-612.
PubMed=15175154; DOI=10.1016/j.molcel.2004.05.005;
Brumbaugh K.M., Otterness D.M., Geisen C., Oliveira V., Brognard J.,
Li X., Lejeune F., Tibbetts R.S., Maquat L.E., Abraham R.T.;
"The mRNA surveillance protein hSMG-1 functions in genotoxic stress
response pathways in mammalian cells.";
Mol. Cell 14:585-598(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-3661.
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[7]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2878-3661, TISSUE SPECIFICITY, AND
INTERACTION WITH PRKCI.
PubMed=8524286; DOI=10.1128/MCB.16.1.105;
Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J.;
"Lambda-interacting protein, a novel protein that specifically
interacts with the zinc finger domain of the atypical protein kinase C
isotype lambda/iota and stimulates its kinase activity in vitro and in
vivo.";
Mol. Cell. Biol. 16:105-114(1996).
[9]
DUPLICATION.
PubMed=11948212; DOI=10.1093/jhered/92.6.462;
Eichler E.E., Johnson M.E., Alkan C., Tuzun E., Sahinalp C.,
Misceo D., Archidiacono N., Rocchi M.;
"Divergent origins and concerted expansion of two segmental
duplications on chromosome 16.";
J. Hered. 92:462-468(2001).
[10]
INTERACTION WITH SMG5.
PubMed=14636577; DOI=10.1016/S1097-2765(03)00443-X;
Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R.,
Grimson A., Hachiya T., Hentze M.W., Anderson P., Ohno S.;
"Phosphorylation of hUPF1 induces formation of mRNA surveillance
complexes containing hSMG-5 and hSMG-7.";
Mol. Cell 12:1187-1200(2003).
[11]
INTERACTION WITH RENT1; UPF2; EST1A AND UPF3B.
PubMed=12554878; DOI=10.1261/rna.2137903;
Chiu S.-Y., Serin G., Ohara O., Maquat L.E.;
"Characterization of human Smg5/7a: a protein with similarities to
Caenorhabditis elegans SMG5 and SMG7 that functions in the
dephosphorylation of Upf1.";
RNA 9:77-87(2003).
[12]
FUNCTION, INTERACTION WITH UPF2, AND IDENTIFICATION IN THE SURF
COMPLEX.
PubMed=16452507; DOI=10.1101/gad.1389006;
Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R.,
Hoshino S., Ohno M., Dreyfuss G., Ohno S.;
"Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon
junction complex triggers Upf1 phosphorylation and nonsense-mediated
mRNA decay.";
Genes Dev. 20:355-367(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550 AND SER-3556, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3570, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE SMG1C COMPLEX.
PubMed=19417104; DOI=10.1101/gad.1767209;
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B.,
Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T.,
Kurata R., Hirano H., Anderson P., Ohno S.;
"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
remodeling of the mRNA surveillance complex during nonsense-mediated
mRNA decay.";
Genes Dev. 23:1091-1105(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
INTERACTION WITH TELO2 AND TTI1.
PubMed=20427287; DOI=10.1074/jbc.M110.121699;
Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
Iemura S., Natsume T., Mizushima N.;
"Tti1 and Tel2 are critical factors in mammalian target of rapamycin
complex assembly.";
J. Biol. Chem. 285:20109-20116(2010).
[21]
INTERACTION WITH TTI1.
PubMed=20810650; DOI=10.1101/gad.1934210;
Hurov K.E., Cotta-Ramusino C., Elledge S.J.;
"A genetic screen identifies the Triple T complex required for DNA
damage signaling and ATM and ATR stability.";
Genes Dev. 24:1939-1950(2010).
[22]
INTERACTION WITH RUVBL1 AND RUVBL2.
PubMed=20371770; DOI=10.1126/scisignal.2000468;
Izumi N., Yamashita A., Iwamatsu A., Kurata R., Nakamura H., Saari B.,
Hirano H., Anderson P., Ohno S.;
"AAA+ proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function
in nonsense-mediated mRNA decay.";
Sci. Signal. 3:RA27-RA27(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
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).
[25]
INTERACTION WITH SMG8 AND SMG9, AND ELECTRON MICROSCOPY OF THE SMG1C
COMPLEX.
PubMed=21245168; DOI=10.1101/gad.606911;
Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R.,
Bamba Y., Izumi N., Ohno S., Llorca O.;
"The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-
scale conformational changes controlled by SMG-8.";
Genes Dev. 25:153-164(2011).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550; SER-3556; SER-3570
AND THR-3573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
VARIANTS [LARGE SCALE ANALYSIS] THR-35; CYS-126; CYS-144; TYR-151;
ASN-160; VAL-167; GLY-320; SER-465; ARG-546; SER-588; LYS-612;
CYS-753; CYS-809; CYS-812; ILE-829; ASP-832; GLY-952; SER-969;
LEU-1016; GLN-1029; SER-1072; HIS-1103; ARG-1275; PRO-1292; VAL-1332;
PRO-1358; THR-1418; CYS-2171; SER-2258; LYS-2345; GLU-2730; SER-2889;
ALA-2899; THR-3239 AND GLN-3583.
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).
-!- FUNCTION: Serine/threonine protein kinase involved in both mRNA
surveillance and genotoxic stress response pathways. Recognizes
the substrate consensus sequence [ST]-Q. Plays a central role in
nonsense-mediated decay (NMD) of mRNAs containing premature stop
codons by phosphorylating UPF1/RENT1. Recruited by release factors
to stalled ribosomes together with SMG8 and SMG9 (forming the
SMG1C protein kinase complex), and UPF1 to form the transient SURF
(SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF
complex associates with the exon junction complex (EJC) through
UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance
complex which is believed to activate NMD. Also acts as a
genotoxic stress-activated protein kinase that displays some
functional overlap with ATM. Can phosphorylate p53/TP53 and is
required for optimal p53/TP53 activation after cellular exposure
to genotoxic stress. Its depletion leads to spontaneous DNA damage
and increased sensitivity to ionizing radiation (IR). May activate
PRKCI but not PRKCZ. {ECO:0000269|PubMed:11331269,
ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:15175154,
ECO:0000269|PubMed:16452507}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:19417104}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11331269};
-!- ENZYME REGULATION: Inhibited by caffeine, LY294002 and wortmannin.
{ECO:0000269|PubMed:11331269, ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:15175154}.
-!- SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and
SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large
conformational change in the SMG1 C-terminal head domain
containing the catalytic domain. Component of the transient SURF
(SMG1-UPF1-eRF1-eRF3) complex. Interacts with PRKCI. Interacts
with TELO2 and TTI1. Interacts with RUVBL1 and RUVBL2. Interacts
with UPF2. {ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:12554878, ECO:0000269|PubMed:14636577,
ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:19417104,
ECO:0000269|PubMed:20371770, ECO:0000269|PubMed:20427287,
ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:21245168,
ECO:0000269|PubMed:8524286}.
-!- INTERACTION:
P11940:PABPC1; NbExp=2; IntAct=EBI-1049832, EBI-81531;
Q9HAU5:UPF2; NbExp=7; IntAct=EBI-1049832, EBI-372073;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15175154}.
Cytoplasm {ECO:0000269|PubMed:15175154}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96Q15-1; Sequence=Displayed;
Name=2;
IsoId=Q96Q15-2; Sequence=VSP_017748;
Name=3;
IsoId=Q96Q15-3; Sequence=VSP_017747;
Name=4; Synonyms=BLIP;
IsoId=Q96Q15-4; Sequence=VSP_017746;
-!- TISSUE SPECIFICITY: Widely expressed, with highest level in heart
and skeletal muscle. Expressed in placenta, brain, lung and
spleen, but not in liver. {ECO:0000269|PubMed:15175154,
ECO:0000269|PubMed:8524286}.
-!- PTM: Autophosphorylated. {ECO:0000305|PubMed:11331269,
ECO:0000305|PubMed:11544179, ECO:0000305|PubMed:15175154}.
-!- MISCELLANEOUS: This gene is located in a region of chromosome 16
that contains 2 segmental duplications. Other genes that are
highly related to this exist, but they probably represent
pseudogenes.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA86535.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF186377; AAK58892.1; -; mRNA.
EMBL; AB061371; BAB70696.1; -; mRNA.
EMBL; AY014957; AAK00511.1; -; mRNA.
EMBL; AF395444; AAM73708.1; -; mRNA.
EMBL; AC092287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB007881; BAA24851.2; -; mRNA.
EMBL; U32581; AAA86535.2; ALT_INIT; mRNA.
CCDS; CCDS45430.1; -. [Q96Q15-1]
PIR; JC6084; JC6084.
RefSeq; NP_055907.3; NM_015092.4. [Q96Q15-1]
UniGene; Hs.460179; -.
ProteinModelPortal; Q96Q15; -.
BioGrid; 116687; 32.
CORUM; Q96Q15; -.
IntAct; Q96Q15; 31.
MINT; MINT-1513197; -.
STRING; 9606.ENSP00000402515; -.
BindingDB; Q96Q15; -.
ChEMBL; CHEMBL1795195; -.
GuidetoPHARMACOLOGY; 2201; -.
iPTMnet; Q96Q15; -.
PhosphoSitePlus; Q96Q15; -.
BioMuta; SMG1; -.
DMDM; 322510104; -.
EPD; Q96Q15; -.
MaxQB; Q96Q15; -.
PaxDb; Q96Q15; -.
PeptideAtlas; Q96Q15; -.
PRIDE; Q96Q15; -.
Ensembl; ENST00000446231; ENSP00000402515; ENSG00000157106. [Q96Q15-1]
GeneID; 23049; -.
KEGG; hsa:23049; -.
UCSC; uc002dfm.4; human. [Q96Q15-1]
CTD; 23049; -.
DisGeNET; 23049; -.
EuPathDB; HostDB:ENSG00000157106.16; -.
GeneCards; SMG1; -.
H-InvDB; HIX0012849; -.
H-InvDB; HIX0038625; -.
H-InvDB; HIX0202313; -.
HGNC; HGNC:30045; SMG1.
HPA; HPA006870; -.
HPA; HPA031623; -.
HPA; HPA073972; -.
MIM; 607032; gene.
neXtProt; NX_Q96Q15; -.
OpenTargets; ENSG00000157106; -.
PharmGKB; PA164725852; -.
eggNOG; KOG0891; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00890000139466; -.
HOGENOM; HOG000168703; -.
HOVERGEN; HBG093965; -.
InParanoid; Q96Q15; -.
KO; K08873; -.
OMA; PWKVIIP; -.
OrthoDB; EOG091G0072; -.
PhylomeDB; Q96Q15; -.
TreeFam; TF352560; -.
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNOR; Q96Q15; -.
ChiTaRS; SMG1; human.
GeneWiki; SMG1_(gene); -.
GenomeRNAi; 23049; -.
PRO; PR:Q96Q15; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000157106; -.
ExpressionAtlas; Q96Q15; baseline and differential.
Genevisible; Q96Q15; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; TAS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0006406; P:mRNA export from nucleus; TAS:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0006950; P:response to stress; IDA:UniProtKB.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR003152; FATC_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR031559; SMG1.
InterPro; IPR035175; SMG1_N.
Pfam; PF17229; DUF5303; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF15785; SMG1; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 5.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; DNA damage; DNA repair; Kinase; Manganese; Metal-binding;
Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 3661 Serine/threonine-protein kinase SMG1.
/FTId=PRO_0000229791.
DOMAIN 1131 1866 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
REPEAT 1817 1852 HEAT.
DOMAIN 2150 2478 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 3629 3661 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
REGION 1 1977 Interaction with SMG8 and SMG9.
{ECO:0000269|PubMed:21245168}.
MOD_RES 173 173 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 3550 3550 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 3556 3556 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 3570 3570 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 3573 3573 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 3577 3577 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BKX6}.
VAR_SEQ 1 1269 Missing (in isoform 4).
{ECO:0000303|PubMed:9566925}.
/FTId=VSP_017746.
VAR_SEQ 1 630 Missing (in isoform 3).
{ECO:0000303|PubMed:11331269}.
/FTId=VSP_017747.
VAR_SEQ 1 140 Missing (in isoform 2).
{ECO:0000303|PubMed:15175154}.
/FTId=VSP_017748.
VARIANT 35 35 A -> T (in dbSNP:rs12051350).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041623.
VARIANT 126 126 R -> C (in dbSNP:rs752796432).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041624.
VARIANT 144 144 S -> C (in dbSNP:rs766737607).
{ECO:0000269|PubMed:15175154,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_041625.
VARIANT 151 151 N -> Y (in dbSNP:rs750788715).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041626.
VARIANT 160 160 D -> N. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041627.
VARIANT 167 167 A -> V. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041628.
VARIANT 320 320 D -> G. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041629.
VARIANT 465 465 G -> S (in dbSNP:rs200419100).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041630.
VARIANT 546 546 H -> R (in dbSNP:rs376234691).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041631.
VARIANT 588 588 A -> S (in dbSNP:rs750840136).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041632.
VARIANT 612 612 I -> K (in dbSNP:rs17842615).
{ECO:0000269|PubMed:15175154,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_041633.
VARIANT 753 753 S -> C (in dbSNP:rs569679854).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041634.
VARIANT 809 809 S -> C. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041635.
VARIANT 812 812 R -> C. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041636.
VARIANT 829 829 V -> I. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041637.
VARIANT 832 832 N -> D (in dbSNP:rs192246457).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041638.
VARIANT 952 952 A -> G (in dbSNP:rs555078480).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041639.
VARIANT 969 969 N -> S. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041640.
VARIANT 1016 1016 F -> L. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041641.
VARIANT 1029 1029 R -> Q. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041642.
VARIANT 1072 1072 T -> S (in dbSNP:rs45516593).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041643.
VARIANT 1103 1103 N -> H (in dbSNP:rs563883658).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041644.
VARIANT 1275 1275 P -> R. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041645.
VARIANT 1292 1292 Q -> P. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041646.
VARIANT 1332 1332 I -> V. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041647.
VARIANT 1358 1358 S -> P. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041648.
VARIANT 1418 1418 R -> T (in dbSNP:rs17731779).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041649.
VARIANT 2171 2171 S -> C (in a breast pleomorphic lobular
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041650.
VARIANT 2258 2258 G -> S (in dbSNP:rs35572280).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041651.
VARIANT 2345 2345 M -> K (in dbSNP:rs56276814).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041652.
VARIANT 2730 2730 Q -> E (in dbSNP:rs34960798).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041653.
VARIANT 2889 2889 G -> S (in dbSNP:rs35952340).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041654.
VARIANT 2899 2899 P -> A (in dbSNP:rs55782217).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041655.
VARIANT 3239 3239 I -> T (in a breast infiltrating ductal
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041656.
VARIANT 3583 3583 K -> Q (in a breast infiltrating ductal
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041657.
MUTAGEN 2335 2335 D->A: Loss of function.
{ECO:0000269|PubMed:11331269,
ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:15175154}.
CONFLICT 14 14 G -> GGGGG (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 20 20 K -> N (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 22 22 P -> S (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 40 40 D -> G (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 686 686 S -> A (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 743 743 K -> R (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 1193 1193 C -> F (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 2009 2009 K -> R (in Ref. 2; BAB70696).
{ECO:0000305}.
CONFLICT 2077 2077 S -> N (in Ref. 1; AAK58892).
{ECO:0000305}.
SEQUENCE 3661 AA; 410501 MW; 216A55F3121F5829 CRC64;
MSRRAPGSRL SSGGGGGGTK YPRSWNDWQP RTDSASADPD NLKYSSSRDR GGSSSYGLQP
SNSAVVSRQR HDDTRVHADI QNDEKGGYSV NGGSGENTYG RKSLGQELRV NNVTSPEFTS
VQHGSRALAT KDMRKSQERS MSYSDESRLS NLLRRITRED DRDRRLATVK QLKEFIQQPE
NKLVLVKQLD NILAAVHDVL NESSKLLQEL RQEGACCLGL LCASLSYEAE KIFKWIFSKF
SSSAKDEVKL LYLCATYKAL ETVGEKKAFS SVMQLVMTSL QSILENVDTP ELLCKCVKCI
LLVARCYPHI FSTNFRDTVD ILVGWHIDHT QKPSLTQQVS GWLQSLEPFW VADLAFSTTL
LGQFLEDMEA YAEDLSHVAS GESVDEDVPP PSVSLPKLAA LLRVFSTVVR SIGERFSPIR
GPPITEAYVT DVLYRVMRCV TAANQVFFSE AVLTAANECV GVLLGSLDPS MTIHCDMVIT
YGLDQLENCQ TCGTDYIISV LNLLTLIVEQ INTKLPSSFV EKLFIPSSKL LFLRYHKEKE
VVAVAHAVYQ AVLSLKNIPV LETAYKLILG EMTCALNNLL HSLQLPEACS EIKHEAFKNH
VFNVDNAKFV VIFDLSALTT IGNAKNSLIG MWALSPTVFA LLSKNLMIVH SDLAVHFPAI
QYAVLYTLYS HCTRHDHFIS SSLSSSSPSL FDGAVISTVT TATKKHFSII LNLLGILLKK
DNLNQDTRKL LMTWALEAAV LMKKSETYAP LFSLPSFHKF CKGLLANTLV EDVNICLQAC
SSLHALSSSL PDDLLQRCVD VCRVQLVHSG TRIRQAFGKL LKSIPLDVVL SNNNHTEIQE
ISLALRSHMS KAPSNTFHPQ DFSDVISFIL YGNSHRTGKD NWLERLFYSC QRLDKRDQST
IPRNLLKTDA VLWQWAIWEA AQFTVLSKLR TPLGRAQDTF QTIEGIIRSL AAHTLNPDQD
VSQWTTADND EGHGNNQLRL VLLLQYLENL EKLMYNAYEG CANALTSPPK VIRTFFYTNR
QTCQDWLTRI RLSIMRVGLL AGQPAVTVRH GFDLLTEMKT TSLSQGNELE VTIMMVVEAL
CELHCPEAIQ GIAVWSSSIV GKNLLWINSV AQQAEGRFEK ASVEYQEHLC AMTGVDCCIS
SFDKSVLTLA NAGRNSASPK HSLNGESRKT VLSKPTDSSP EVINYLGNKA CECYISIADW
AAVQEWQNAI HDLKKSTSST SLNLKADFNY IKSLSSFESG KFVECTEQLE LLPGENINLL
AGGSKEKIDM KKLLPNMLSP DPRELQKSIE VQLLRSSVCL ATALNPIEQD QKWQSITENV
VKYLKQTSRI AIGPLRLSTL TVSQSLPVLS TLQLYCSSAL ENTVSNRLST EDCLIPLFSE
ALRSCKQHDV RPWMQALRYT MYQNQLLEKI KEQTVPIRSH LMELGLTAAK FARKRGNVSL
ATRLLAQCSE VQLGKTTTAQ DLVQHFKKLS TQGQVDEKWG PELDIEKTKL LYTAGQSTHA
MEMLSSCAIS FCKSVKAEYA VAKSILTLAK WIQAEWKEIS GQLKQVYRAQ HQQNFTGLST
LSKNILTLIE LPSVNTMEEE YPRIESESTV HIGVGEPDFI LGQLYHLSSV QAPEVAKSWA
ALASWAYRWG RKVVDNASQG EGVRLLPREK SEVQNLLPDT ITEEEKERIY GILGQAVCRP
AGIQDEDITL QITESEDNEE DDMVDVIWRQ LISSCPWLSE LDESATEGVI KVWRKVVDRI
FSLYKLSCSA YFTFLKLNAG QIPLDEDDPR LHLSHRVEQS TDDMIVMATL RLLRLLVKHA
GELRQYLEHG LETTPTAPWR GIIPQLFSRL NHPEVYVRQS ICNLLCRVAQ DSPHLILYPA
IVGTISLSSE SQASGNKFST AIPTLLGNIQ GEELLVSECE GGSPPASQDS NKDEPKSGLN
EDQAMMQDCY SKIVDKLSSA NPTMVLQVQM LVAELRRVTV LWDELWLGVL LQQHMYVLRR
IQQLEDEVKR VQNNNTLRKE EKIAIMREKH TALMKPIVFA LEHVRSITAA PAETPHEKWF
QDNYGDAIEN ALEKLKTPLN PAKPGSSWIP FKEIMLSLQQ RAQKRASYIL RLEEISPWLA
AMTNTEIALP GEVSARDTVT IHSVGGTITI LPTKTKPKKL LFLGSDGKSY PYLFKGLEDL
HLDERIMQFL SIVNTMFATI NRQETPRFHA RHYSVTPLGT RSGLIQWVDG ATPLFGLYKR
WQQREAALQA QKAQDSYQTP QNPGIVPRPS ELYYSKIGPA LKTVGLSLDV SRRDWPLHVM
KAVLEELMEA TPPNLLAKEL WSSCTTPDEW WRVTQSYARS TAVMSMVGYI IGLGDRHLDN
VLIDMTTGEV VHIDYNVCFE KGKSLRVPEK VPFRMTQNIE TALGVTGVEG VFRLSCEQVL
HIMRRGRETL LTLLEAFVYD PLVDWTAGGE AGFAGAVYGG GGQQAESKQS KREMEREITR
SLFSSRVAEI KVNWFKNRDE MLVVLPKLDG SLDEYLSLQE QLTDVEKLQG KLLEEIEFLE
GAEGVDHPSH TLQHRYSEHT QLQTQQRAVQ EAIQVKLNEF EQWITHYQAA FNNLEATQLA
SLLQEISTQM DLGPPSYVPA TAFLQNAGQA HLISQCEQLE GEVGALLQQR RSVLRGCLEQ
LHHYATVALQ YPKAIFQKHR IEQWKTWMEE LICNTTVERC QELYRKYEMQ YAPQPPPTVC
QFITATEMTL QRYAADINSR LIRQVERLKQ EAVTVPVCED QLKEIERCIK VFLHENGEEG
SLSLASVIIS ALCTLTRRNL MMEGAASSAG EQLVDLTSRD GAWFLEELCS MSGNVTCLVQ
LLKQCHLVPQ DLDIPNPMEA SETVHLANGV YTSLQELNSN FRQIIFPEAL RCLMKGEYTL
ESMLHELDGL IEQTTDGVPL QTLVESLQAY LRNAAMGLEE ETHAHYIDVA RLLHAQYGEL
IQPRNGSVDE TPKMSAGQML LVAFDGMFAQ VETAFSLLVE KLNKMEIPIA WRKIDIIREA
RSTQVNFFDD DNHRQVLEEI FFLKRLQTIK EFFRLCGTFS KTLSGSSSLE DQNTVNGPVQ
IVNVKTLFRN SCFSEDQMAK PIKAFTADFV RQLLIGLPNQ ALGLTLCSFI SALGVDIIAQ
VEAKDFGAES KVSVDDLCKK AVEHNIQIGK FSQLVMNRAT VLASSYDTAW KKHDLVRRLE
TSISSCKTSL QRVQLHIAMF QWQHEDLLIN RPQAMSVTPP PRSAILTSMK KKLHTLSQIE
TSIATVQEKL AALESSIEQR LKWAGGANPA LAPVLQDFEA TIAERRNLVL KESQRASQVT
FLCSNIIHFE SLRTRTAEAL NLDAALFELI KRCQQMCSFA SQFNSSVSEL ELRLLQRVDT
GLEHPIGSSE WLLSAHKQLT QDMSTQRAIQ TEKEQQIETV CETIQNLVDN IKTVLTGHNR
QLGDVKHLLK AMAKDEEAAL ADGEDVPYEN SVRQFLGEYK SWQDNIQTVL FTLVQAMGQV
RSQEHVEMLQ EITPTLKELK TQSQSIYNNL VSFASPLVTD ATNECSSPTS SATYQPSFAA
AVRSNTGQKT QPDVMSQNAR KLIQKNLATS ADTPPSTVPG TGKSVACSPK KAVRDPKTGK
AVQERNSYAV SVWKRVKAKL EGRDVDPNRR MSVAEQVDYV IKEATNLDNL AQLYEGWTAW
V


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