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Kinase suppressor of Ras 1 (mKSR1) (Protein Hb)

 KSR1_MOUSE              Reviewed;         873 AA.
Q61097; Q61648; Q78DX8;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 161.
RecName: Full=Kinase suppressor of Ras 1;
Short=mKSR1;
AltName: Full=Protein Hb;
Name=Ksr1; Synonyms=Ksr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8521512; DOI=10.1016/0092-8674(95)90204-X;
Therrien M., Chang H.C., Solomon N.M., Karim F.D., Wassarman D.A.,
Rubin G.M.;
"KSR, a novel protein kinase required for RAS signal transduction.";
Cell 83:879-888(1995).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), INTERACTION WITH MAPK,
MUTAGENESIS OF GLY-572; ARG-589; ARG-615; ASP-700 AND CYS-809, AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10891492; DOI=10.1128/MCB.20.15.5529-5539.2000;
Mueller J., Cacace A.M., Lyons W.E., McGill C.B., Morrison D.K.;
"Identification of B-KSR1, a novel brain-specific isoform of KSR1 that
functions in neuronal signaling.";
Mol. Cell. Biol. 20:5529-5539(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Pelan S.;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-474 (ISOFORMS 1/2).
STRAIN=BALB/cJ;
PubMed=7626882; DOI=10.1007/BF00364794;
Nehls M., Luno K., Schorpp M., Pfeifer D., Krause S.,
Matysiak-Scholze U., Dierbach H., Boehm T.;
"YAC/P1 contigs defining the location of 56 microsatellite markers and
several genes across a 3.4cM interval on mouse chromosome 11.";
Mamm. Genome 6:321-331(1995).
[5]
FUNCTION, INTERACTION WITH MAP2K1; MAP2K2; HSP90AA1; YWHAE AND CDC37,
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 56-LEU--ARG-57;
GLY-580; ARG-589; ARG-615 AND CYS-809.
PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
"Kinase suppressor of Ras forms a multiprotein signaling complex and
modulates MEK localization.";
Mol. Cell. Biol. 19:5523-5534(1999).
[6]
INTERACTION WITH MARK3, PHOSPHORYLATION AT SER-297 AND SER-392,
MUTAGENESIS OF SER-297; SER-392; ILE-397 AND VAL-401, AND SUBCELLULAR
LOCATION.
PubMed=11741534; DOI=10.1016/S1097-2765(01)00383-5;
Mueller J., Ory S., Copeland T., Piwnica-Worms H., Morrison D.K.;
"C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold,
KSR1.";
Mol. Cell 8:983-993(2001).
[7]
FUNCTION, INTERACTION WITH PPP2R1A AND PPP2CA, DEPHOSPHORYLATION BY
PPP2CA, AND SUBCELLULAR LOCATION.
PubMed=12932319; DOI=10.1016/S0960-9822(03)00535-9;
Ory S., Zhou M., Conrads T.P., Veenstra T.D., Morrison D.K.;
"Protein phosphatase 2A positively regulates Ras signaling by
dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites.";
Curr. Biol. 13:1356-1364(2003).
[8]
REVIEW.
PubMed=12007434; DOI=10.1016/S0960-9822(02)00831-X;
Roy F., Therrien M.;
"MAP kinase module: the Ksr connection.";
Curr. Biol. 12:R325-R327(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-392 AND
SER-518, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, INTERACTION WITH AKAP13; MAP2K1 AND BRAF, IDENTIFICATION BY
MASS SPECTROMETRY, PHOSPHORYLATION AT SER-838, AND MUTAGENESIS OF
SER-838.
PubMed=21102438; DOI=10.1038/ncb2130;
Smith F.D., Langeberg L.K., Cellurale C., Pawson T., Morrison D.K.,
Davis R.J., Scott J.D.;
"AKAP-Lbc enhances cyclic AMP control of the ERK1/2 cascade.";
Nat. Cell Biol. 12:1242-1249(2010).
[11]
STRUCTURE BY NMR OF 331-378 IN COMPLEX WITH ZINC.
PubMed=11786023; DOI=10.1006/jmbi.2001.5263;
Zhou M., Horita D.A., Waugh D.S., Byrd R.A., Morrison D.K.;
"Solution structure and functional analysis of the cysteine-rich C1
domain of kinase suppressor of Ras (KSR).";
J. Mol. Biol. 315:435-446(2002).
[12] {ECO:0000244|PDB:2LPE}
STRUCTURE BY NMR OF 25-170, INTERACTION WITH BRAF AND MAP2K1, DOMAIN,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 56-LEU-ARG-57; ILE-71 AND
LEU-78.
PubMed=23250398; DOI=10.1126/scisignal.2003289;
Koveal D., Schuh-Nuhfer N., Ritt D., Page R., Morrison D.K., Peti W.;
"A CC-SAM, for coiled coil-sterile alpha motif, domain targets the
scaffold KSR-1 to specific sites in the plasma membrane.";
Sci. Signal. 5:RA94-RA94(2012).
-!- FUNCTION: Scaffolding protein that is part of a multiprotein
signaling complex. Promotes phosphorylation of Raf family members
and activation of downstream MAP kinases (PubMed:10409742,
PubMed:12932319, PubMed:21102438). Promotes activation of MAPK1
and/or MAPK3, both in response to EGF and to cAMP
(PubMed:21102438). Does not have kinase activity by itself
(Probable). {ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:21102438,
ECO:0000305}.
-!- SUBUNIT: Interacts with HSP90AA1/HSP90, YWHAB/14-3-3, CDC37,
MAP2K1/MEK-1, MAP2K2/MEK-2, MARK3, PPP2R1A and PPP2CA
(PubMed:10891492, PubMed:10409742, PubMed:11741534,
PubMed:12932319). Interacts with YWHAE (PubMed:10409742). Also
interacts with RAF and MAPK/ERK, in a Ras-dependent manner. The
binding of 14-3-3 proteins to phosphorylated KSR prevents the
membrane localization (PubMed:8521512). Interacts with VRK2 (By
similarity). Interacts with AKAP13 and BRAF. Identified in a
complex with AKAP13, MAP2K1 and BRAF (PubMed:21102438,
PubMed:23250398). {ECO:0000250|UniProtKB:Q8IVT5,
ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:21102438,
ECO:0000269|PubMed:23250398}.
-!- INTERACTION:
Q60875:Arhgef2; NbExp=5; IntAct=EBI-1536336, EBI-772191;
P15056:BRAF (xeno); NbExp=3; IntAct=EBI-1536336, EBI-365980;
P15531:NME1 (xeno); NbExp=7; IntAct=EBI-1536336, EBI-741141;
Q86Y07-1:VRK2 (xeno); NbExp=8; IntAct=EBI-1536336, EBI-1207633;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319,
ECO:0000269|PubMed:23250398}. Membrane
{ECO:0000269|PubMed:10409742}; Peripheral membrane protein
{ECO:0000269|PubMed:10409742}. Cell membrane
{ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319,
ECO:0000269|PubMed:23250398}; Peripheral membrane protein
{ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319,
ECO:0000269|PubMed:23250398}. Cell projection, ruffle membrane
{ECO:0000269|PubMed:23250398}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q8IVT5}. Note=In unstimulated cells, where
the phosphorylated form is bound to a 14-3-3 protein,
sequestration in the cytoplasm occurs. Following growth factor
treatment, the protein is free for membrane translocation, and it
moves from the cytoplasm to the cell periphery.
{ECO:0000305|PubMed:12932319}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q61097-1; Sequence=Displayed;
Name=2; Synonyms=B-KSR1;
IsoId=Q61097-2; Sequence=VSP_012232, VSP_012233;
-!- TISSUE SPECIFICITY: Expressed in brain, spleen and testis. Isoform
1 is highly expressed spleen and weakly in testis, and isoform 2
is highly expressed in brain and weakly in testis.
{ECO:0000269|PubMed:10891492}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive. The domain is sufficient for KSR1 and KSR1-mediated
MAP2K1 and MAP2K2 membrane localization. The domain is required
but not sufficient for MAP kinase-mediated inhibition of ELK1
phosphorylation (PubMed:10409742). {ECO:0000255,
ECO:0000269|PubMed:10409742}.
-!- DOMAIN: The N-terminal region mediates interaction with BRAF and
with membranes. {ECO:0000269|PubMed:23250398}.
-!- PTM: Phosphorylated on Ser-297 and, to a higher extent, on Ser-392
by MARK3 (PubMed:11741534). Dephosphorylated on Ser-392 by PPP2CA
(PubMed:12932319). Phosphorylated KSR1 is cytoplasmic and
dephosphorylated KSR1 is membrane-associated (Probable).
Phosphorylated by PKA at Ser-838. Phosphorylation at Ser-838 is
required for cAMP-dependent activation of MAPK1 and/or MAPK3
(PubMed:21102438). {ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:10891492, ECO:0000269|PubMed:11741534,
ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:21102438,
ECO:0000305}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
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EMBL; U43585; AAC52382.1; -; mRNA.
EMBL; AL592551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X81634; CAA57288.1; -; mRNA.
CCDS; CCDS25117.1; -. [Q61097-1]
PIR; I48379; I48379.
RefSeq; NP_001335136.1; NM_001348207.1.
RefSeq; NP_038599.1; NM_013571.3. [Q61097-1]
RefSeq; XP_006532398.1; XM_006532335.3. [Q61097-2]
UniGene; Mm.4745; -.
PDB; 1KBE; NMR; -; A=331-378.
PDB; 1KBF; NMR; -; A=331-378.
PDB; 2LPE; NMR; -; A=25-170.
PDBsum; 1KBE; -.
PDBsum; 1KBF; -.
PDBsum; 2LPE; -.
ProteinModelPortal; Q61097; -.
SMR; Q61097; -.
BioGrid; 201048; 238.
CORUM; Q61097; -.
IntAct; Q61097; 8.
MINT; Q61097; -.
STRING; 10090.ENSMUSP00000018478; -.
iPTMnet; Q61097; -.
PhosphoSitePlus; Q61097; -.
EPD; Q61097; -.
PaxDb; Q61097; -.
PeptideAtlas; Q61097; -.
PRIDE; Q61097; -.
DNASU; 16706; -.
Ensembl; ENSMUST00000018478; ENSMUSP00000018478; ENSMUSG00000018334. [Q61097-1]
GeneID; 16706; -.
KEGG; mmu:16706; -.
UCSC; uc033fyo.1; mouse. [Q61097-1]
CTD; 8844; -.
MGI; MGI:105051; Ksr1.
eggNOG; KOG0193; Eukaryota.
eggNOG; ENOG410Y4UP; LUCA.
GeneTree; ENSGT00900000140880; -.
HOGENOM; HOG000113263; -.
HOVERGEN; HBG052293; -.
InParanoid; Q61097; -.
KO; K14958; -.
OMA; SDTCIPL; -.
OrthoDB; EOG091G02ZN; -.
PhylomeDB; Q61097; -.
TreeFam; TF317006; -.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-5674135; MAP2K and MAPK activation.
Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
EvolutionaryTrace; Q61097; -.
PRO; PR:Q61097; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018334; -.
CleanEx; MM_KSR1; -.
ExpressionAtlas; Q61097; baseline and differential.
Genevisible; Q61097; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0071889; F:14-3-3 protein binding; IPI:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0043405; P:regulation of MAP kinase activity; IMP:UniProtKB.
CDD; cd00029; C1; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR025561; KSR_SAM-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF13543; KSR1-SAM; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00109; C1; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 873 Kinase suppressor of Ras 1.
/FTId=PRO_0000086230.
DOMAIN 563 833 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 333 377 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 1 170 Mediates association with membranes.
{ECO:0000269|PubMed:23250398}.
COMPBIAS 17 21 Poly-Gly.
COMPBIAS 275 278 Poly-Pro.
COMPBIAS 429 491 Ser-rich.
METAL 334 334 Zinc 1. {ECO:0000269|PubMed:11786023}.
METAL 346 346 Zinc 2. {ECO:0000269|PubMed:11786023}.
METAL 349 349 Zinc 2. {ECO:0000269|PubMed:11786023}.
METAL 359 359 Zinc 1. {ECO:0000269|PubMed:11786023}.
METAL 362 362 Zinc 1. {ECO:0000269|PubMed:11786023}.
METAL 367 367 Zinc 2. {ECO:0000269|PubMed:11786023}.
METAL 370 370 Zinc 2. {ECO:0000269|PubMed:11786023}.
METAL 377 377 Zinc 1. {ECO:0000269|PubMed:11786023}.
MOD_RES 256 256 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IVT5}.
MOD_RES 260 260 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IVT5}.
MOD_RES 297 297 Phosphoserine; by MARK3.
{ECO:0000269|PubMed:11741534}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IVT5}.
MOD_RES 392 392 Phosphoserine; by MARK3.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:11741534}.
MOD_RES 411 411 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IVT5}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000269|PubMed:21102438}.
VAR_SEQ 474 474 P -> PAAYFIHHRQQFIFP (in isoform 2).
{ECO:0000305}.
/FTId=VSP_012232.
VAR_SEQ 848 873 DINSSKVMPRFERFGLGTLESGNPKM -> EL (in
isoform 2). {ECO:0000305}.
/FTId=VSP_012233.
MUTAGEN 56 57 LR->GS: No effect on the interaction with
MAP2K1, MAP2K2 and YWHAE. Abolishes
interaction with BRAF. Abolishes location
at membrane ruffles.
{ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:23250398}.
MUTAGEN 71 71 I->A: Impairs interaction with BRAF and
association with membrane ruffles; when
associated with A-78.
{ECO:0000269|PubMed:23250398}.
MUTAGEN 78 78 L->A: Impairs interaction with BRAF and
association with membrane ruffles; when
associated with A-78.
{ECO:0000269|PubMed:23250398}.
MUTAGEN 297 297 S->A: Constitutive targeting to the
plasma membrane; when associated with A-
392. {ECO:0000269|PubMed:11741534}.
MUTAGEN 392 392 S->A: Constitutive targeting to the
plasma membrane; when associated with A-
297. {ECO:0000269|PubMed:11741534}.
MUTAGEN 397 397 I->A: Decrease in MARK3 binding; when
associated with A-401.
{ECO:0000269|PubMed:11741534}.
MUTAGEN 401 401 V->A: Decrease in MARK3 binding; when
associated with A-397.
{ECO:0000269|PubMed:11741534}.
MUTAGEN 572 572 G->E: Decrease in MEK binding.
{ECO:0000269|PubMed:10891492}.
MUTAGEN 580 580 G->E: Partial decrease in MAP2K1 and
MAP2K2 binding. No effect on the
interaction with YWHAE.
{ECO:0000269|PubMed:10409742}.
MUTAGEN 589 589 R->M: Severe decrease in MAP2K1 and
MAP2K2 binding. No effect on the
interaction with YWHAE.
{ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:10891492}.
MUTAGEN 615 615 R->H: Severe decrease in MAP2K1 and
MAP2K2 binding. No effect on the
interaction with YWHAE.
{ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:10891492}.
MUTAGEN 700 700 D->V: Decrease in MEK binding.
{ECO:0000269|PubMed:10891492}.
MUTAGEN 809 809 C->Y: Associates almost exclusively with
the membrane. Loss of MAP2K2 and MAP2K2
binding and recruitment to the membrane.
Loss of MAP kinase-mediated inhibition of
ELK1 phosphorylation. No effect on the
interaction with YWHAE.
{ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:10891492}.
MUTAGEN 838 838 S->A: Abolishes one phosphorylation site.
Decreases phosphorylation by PKA.
{ECO:0000269|PubMed:21102438}.
TURN 30 32 {ECO:0000244|PDB:2LPE}.
HELIX 33 36 {ECO:0000244|PDB:2LPE}.
HELIX 37 39 {ECO:0000244|PDB:2LPE}.
HELIX 47 58 {ECO:0000244|PDB:2LPE}.
HELIX 65 82 {ECO:0000244|PDB:2LPE}.
HELIX 83 85 {ECO:0000244|PDB:2LPE}.
HELIX 88 90 {ECO:0000244|PDB:2LPE}.
TURN 94 96 {ECO:0000244|PDB:2LPE}.
HELIX 101 103 {ECO:0000244|PDB:2LPE}.
TURN 108 110 {ECO:0000244|PDB:2LPE}.
HELIX 111 114 {ECO:0000244|PDB:2LPE}.
HELIX 118 121 {ECO:0000244|PDB:2LPE}.
HELIX 130 133 {ECO:0000244|PDB:2LPE}.
HELIX 138 146 {ECO:0000244|PDB:2LPE}.
TURN 147 149 {ECO:0000244|PDB:2LPE}.
HELIX 153 162 {ECO:0000244|PDB:2LPE}.
HELIX 163 167 {ECO:0000244|PDB:2LPE}.
STRAND 336 339 {ECO:0000244|PDB:1KBE}.
STRAND 347 349 {ECO:0000244|PDB:1KBE}.
STRAND 356 359 {ECO:0000244|PDB:1KBE}.
TURN 360 363 {ECO:0000244|PDB:1KBE}.
STRAND 364 369 {ECO:0000244|PDB:1KBE}.
TURN 371 373 {ECO:0000244|PDB:1KBE}.
SEQUENCE 873 AA; 96755 MW; EAEEB23FAE715D94 CRC64;
MDRAALRAAA MGEKKEGGGG GAAADGGAGA AVSRALQQCG QLQKLIDISI GSLRGLRTKC
SVSNDLTQQE IRTLEAKLVK YICKQQQSKL SVTPSDRTAE LNSYPRFSDW LYIFNVRPEV
VQEIPQELTL DALLEMDEAK AKEMLRRWGA STEECSRLQQ ALTCLRKVTG LGGEHKMDSG
WSSTDARDSS LGPPMDMLSS LGRAGASTQG PRSISVSALP ASDSPVPGLS EGLSDSCIPL
HTSGRLTPRA LHSFITPPTT PQLRRHAKLK PPRTPPPPSR KVFQLLPSFP TLTRSKSHES
QLGNRIDDVT PMKFELPHGS PQLVRRDIGL SVTHRFSTKS WLSQVCNVCQ KSMIFGVKCK
HCRLKCHNKC TKEAPACRIT FLPLARLRRT ESVPSDINNP VDRAAEPHFG TLPKALTKKE
HPPAMNLDSS SNPSSTTSST PSSPAPFLTS SNPSSATTPP NPSPGQRDSR FSFPDISACS
QAAPLSSTAD STRLDDQPKT DVLGVHEAEA EEPEAGKSEA EDDEEDEVDD LPSSRRPWRG
PISRKASQTS VYLQEWDIPF EQVELGEPIG QGRWGRVHRG RWHGEVAIRL LEMDGHNQDH
LKLFKKEVMN YRQTRHENVV LFMGACMNPP HLAIITSFCK GRTLHSFVRD PKTSLDINKT
RQIAQEIIKG MGYLHAKGIV HKDLKSKNVF YDNGKVVITD FGLFGISGVV REERRENQLK
LSHDWLCYLA PEIVREMIPG RDEDQLPFSK AADVYAFGTV WYELQARDWP FKHQPAEALI
WQIGSGEGVR RVLASVSLGK EVGEILSACW AFDLQERPSF SLLMDMLERL PKLNRRLSHP
GHFWKSADIN SSKVMPRFER FGLGTLESGN PKM


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32-172 p16 (cyclin-dependent kinase inhibitor 2A, INK4a) is a tumor suppressor protein. It is a specific inhibitor of Cdk 4 _ Cdk 6, and a tumor suppressor involved in the pathogenesis of a variety of malign 0.1 mL
EIAAB08204 CNK homolog protein 2,CNK2,Cnksr2,Connector enhancer of kinase suppressor of ras 2,Connector enhancer of KSR 2,Maguin,Membrane-associated guanylate kinase-interacting protein,Rat,Rattus norvegicus
MCA5406Z MOUSE ANTI HUMAN KINASE SUPPRESSOR OF RAS 2 Azide free, Product Type Monoclonal Antibody, Specificity KINASE SUPPRESSOR OF RAS 2, Target Species Human, Host Mouse, Format Azide Free, Isotypes Ig 0.1 mg
30-622 ING1 is a tumor suppressor protein that can induce cell growth arrest and apoptosis. The protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a componen 0.1 mg
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB31331 PAK-1,Pkn,Pkn1,Prk1,Prkcl1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Rat,Rattus norvegicus,Serine_threonine-protein kinase N1,Seri
EIAAB40138 HCCS1,HCCS-1,Homo sapiens,Human,Human cervical cancer suppressor gene 1 protein,ST20,Suppressor of tumorigenicity 20 protein
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB08208 CNK homolog protein 3,CNK3,Cnksr3,Connector enhancer of kinase suppressor of ras 3,Connector enhancer of KSR 3,Maguin-like protein,Parturition-related protein 4,Prp4,Rat,Rattus norvegicus
EIAAB10579 Colorectal cancer suppressor,DCC,Homo sapiens,Human,IGDCC1,Immunoglobulin superfamily DCC subclass member 1,Netrin receptor DCC,Tumor suppressor protein DCC
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB43851 B-cell chronic lymphocytic leukemia tumor suppressor Leu5,E3 ubiquitin-protein ligase TRIM13,Homo sapiens,Human,LEU5,Leukemia-associated protein 5,Putative tumor suppressor RFP2,Ret finger protein 2,R
EIAAB25784 Angiotensin-II type 2 receptor-interacting protein,AT2 receptor-binding protein,Atbp,Atip,Cctsg1,Coiled-coiled tumor suppressor gene 1 protein,Kiaa1288,Microtubule-associated tumor suppressor 1 homolo
EIAAB25786 Angiotensin-II type 2 receptor-interacting protein,AT2 receptor-binding protein,ATBP,ATIP,GK1,Homo sapiens,Human,KIAA1288,Microtubule-associated tumor suppressor 1,Mitochondrial tumor suppressor 1,MTS
BMDV10102 p16INK4a (Cyclin Dependent Kinase Inhibitor), Tumor Suppressor Protein, 16kD, Clone ZJ11, Mab anti_Human, NO X w_Mouse or Rat; IF_Kinase_WB_IP (native & denatured) 0.5 ml.


 

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