GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Sphingoid long chain base kinase 4 (LCB kinase 4) (EC 2.7.1.91) (Sphinganine kinase 4)

 LCB4_YEAST              Reviewed;         624 AA.
Q12246; D6W2M7;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
13-FEB-2019, entry version 153.
RecName: Full=Sphingoid long chain base kinase 4 {ECO:0000303|PubMed:9677363};
Short=LCB kinase 4 {ECO:0000303|PubMed:9677363};
EC=2.7.1.91 {ECO:0000269|PubMed:9677363};
AltName: Full=Sphinganine kinase 4 {ECO:0000305};
Name=LCB4 {ECO:0000303|PubMed:9677363};
OrderedLocusNames=YOR171C {ECO:0000312|SGD:S000005697};
ORFNames=O3615;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8972579;
DOI=10.1002/(SICI)1097-0061(199612)12:15<1563::AID-YEA44>3.0.CO;2-M;
Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
"Analysis of a 22,956 bp region on the right arm of Saccharomyces
cerevisiae chromosome XV.";
Yeast 12:1563-1573(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9677363; DOI=10.1074/jbc.273.31.19437;
Nagiec M.M., Skrzypek M.S., Nagiec E.E., Lester R.L., Dickson R.C.;
"The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode
sphingoid long chain base kinases.";
J. Biol. Chem. 273:19437-19442(1998).
[5]
FUNCTION.
PubMed=11102354;
Kim S., Fyrst H., Saba J.D.;
"Accumulation of phosphorylated sphingoid long chain bases results in
cell growth inhibition in Saccharomyces cerevisiae.";
Genetics 156:1519-1529(2000).
[6]
FUNCTION.
PubMed=11795842; DOI=10.1007/s00294-001-0259-6;
Zhang X., Skrzypek M.S., Lester R.L., Dickson R.C.;
"Elevation of endogenous sphingolipid long-chain base phosphates kills
Saccharomyces cerevisiae cells.";
Curr. Genet. 40:221-233(2001).
[7]
FUNCTION.
PubMed=11056159; DOI=10.1074/jbc.M007425200;
Jenkins G.M., Hannun Y.A.;
"Role for de novo sphingoid base biosynthesis in the heat-induced
transient cell cycle arrest of Saccharomyces cerevisiae.";
J. Biol. Chem. 276:8574-8581(2001).
[8]
FUNCTION.
PubMed=11278643; DOI=10.1074/jbc.M010221200;
Birchwood C.J., Saba J.D., Dickson R.C., Cunningham K.W.;
"Calcium influx and signaling in yeast stimulated by intracellular
sphingosine 1-phosphate accumulation.";
J. Biol. Chem. 276:11712-11718(2001).
[9]
SUBCELLULAR LOCATION.
PubMed=12459470; DOI=10.1016/S0014-5793(02)03636-0;
Hait N.C., Fujita K., Lester R.L., Dickson R.C.;
"Lcb4p sphingoid base kinase localizes to the Golgi and late
endosomes.";
FEBS Lett. 532:97-102(2002).
[10]
FUNCTION.
PubMed=11967828; DOI=10.1002/yea.861;
Ferguson-Yankey S.R., Skrzypek M.S., Lester R.L., Dickson R.C.;
"Mutant analysis reveals complex regulation of sphingolipid long chain
base phosphates and long chain bases during heat stress in yeast.";
Yeast 19:573-586(2002).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12493772; DOI=10.1074/jbc.M209925200;
Funato K., Lombardi R., Vallee B., Riezman H.;
"Lcb4p is a key regulator of ceramide synthesis from exogenous long
chain sphingoid base in Saccharomyces cerevisiae.";
J. Biol. Chem. 278:7325-7334(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
PHOSPHORYLATION AT SER-451 AND SER-455, AND UBIQUITINATION.
PubMed=15598647; DOI=10.1074/jbc.M410908200;
Iwaki S., Kihara A., Sano T., Igarashi Y.;
"Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal for
the down-regulation of the yeast sphingoid long-chain base kinase Lcb4
during the stationary phase.";
J. Biol. Chem. 280:6520-6527(2005).
[14]
FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=16141212; DOI=10.1074/jbc.M503147200;
Sano T., Kihara A., Kurotsu F., Iwaki S., Igarashi Y.;
"Regulation of the sphingoid long-chain base kinase Lcb4p by
ergosterol and heme: studies in phytosphingosine-resistant mutants.";
J. Biol. Chem. 280:36674-36682(2005).
[15]
PALMITOYLATION AT CYS-43 AND CYS-46.
PubMed=16227572; DOI=10.1128/MCB.25.21.9189-9197.2005;
Kihara A., Kurotsu F., Sano T., Iwaki S., Igarashi Y.;
"Long-chain base kinase Lcb4 Is anchored to the membrane through its
palmitoylation by Akr1.";
Mol. Cell. Biol. 25:9189-9197(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-454 AND
SER-455, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-120; SER-154;
SER-451; SER-454; SER-455 AND SER-460, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Catalyzes the phosphorylation of the sphingoid long
chain bases dihydrosphingosine (DHS or sphinganine) and
phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate
(DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively
(PubMed:9677363, PubMed:11102354, PubMed:11795842,
PubMed:16141212). Involved in the biosynthesis of sphingolipids
and ceramides (PubMed:12493772). Required with LCB3 for an
effective incorporation of DHS into ceramides through a
phosphorylation-dephosphorylation cycle. Involved in heat-induced
transient cell cycle arrest (PubMed:11056159). Accumulation of
phosphorylated sphingoid long chain bases (LCBPs) stimulates
calcium influx and activates calcineurin signaling
(PubMed:11278643). Involved in heat-stress resistance
(PubMed:11967828). {ECO:0000269|PubMed:11056159,
ECO:0000269|PubMed:11102354, ECO:0000269|PubMed:11278643,
ECO:0000269|PubMed:11795842, ECO:0000269|PubMed:11967828,
ECO:0000269|PubMed:12493772, ECO:0000269|PubMed:16141212,
ECO:0000269|PubMed:9677363}.
-!- CATALYTIC ACTIVITY:
Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP +
H(+); Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:76941, ChEBI:CHEBI:84410,
ChEBI:CHEBI:456216; EC=2.7.1.91;
Evidence={ECO:0000269|PubMed:9677363};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.7 uM for sphinganine {ECO:0000269|PubMed:9677363};
KM=25 uM for ATP {ECO:0000269|PubMed:9677363};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12459470,
ECO:0000269|PubMed:16141212}; Peripheral membrane protein
{ECO:0000305}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12493772}; Peripheral membrane protein
{ECO:0000305}. Late endosome membrane
{ECO:0000269|PubMed:12459470}; Peripheral membrane protein
{ECO:0000305}. Golgi apparatus membrane
{ECO:0000269|PubMed:12459470}; Peripheral membrane protein
{ECO:0000305}.
-!- PTM: Phosphorylated by the cyclin-CDKs PCL1-PHO85 and PCL2-PHO85.
Phosphorylation is a prerequisite to ubiquitination. The
phosphorylation level depends on sterol composition and may also
be involved in subcellular location (PubMed:16141212).
{ECO:0000269|PubMed:15598647, ECO:0000269|PubMed:16141212}.
-!- PTM: Ubiquitinated. The ubiquitination leads to degradation in the
vacuole. {ECO:0000269|PubMed:15598647}.
-!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U55021; AAB47416.1; -; Genomic_DNA.
EMBL; Z75078; CAA99378.1; -; Genomic_DNA.
EMBL; BK006948; DAA10943.1; -; Genomic_DNA.
PIR; S67059; S67059.
RefSeq; NP_014814.1; NM_001183590.1.
ProteinModelPortal; Q12246; -.
BioGrid; 34565; 152.
DIP; DIP-2844N; -.
IntAct; Q12246; 3.
MINT; Q12246; -.
STRING; 4932.YOR171C; -.
SwissLipids; SLP:000000109; -.
iPTMnet; Q12246; -.
SwissPalm; Q12246; -.
MaxQB; Q12246; -.
PaxDb; Q12246; -.
PRIDE; Q12246; -.
EnsemblFungi; YOR171C_mRNA; YOR171C_mRNA; YOR171C.
GeneID; 854342; -.
KEGG; sce:YOR171C; -.
EuPathDB; FungiDB:YOR171C; -.
SGD; S000005697; LCB4.
GeneTree; ENSGT00940000167991; -.
HOGENOM; HOG000207396; -.
InParanoid; Q12246; -.
KO; K04718; -.
OMA; FYCGNMA; -.
BioCyc; MetaCyc:YOR171C-MONOMER; -.
BioCyc; YEAST:YOR171C-MONOMER; -.
Reactome; R-SCE-1483206; Glycerophospholipid biosynthesis.
Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
Reactome; R-SCE-1660662; Glycosphingolipid metabolism.
Reactome; R-SCE-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-SCE-5218921; VEGFR2 mediated cell proliferation.
PRO; PR:Q12246; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0071944; C:cell periphery; HDA:SGD.
GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:SGD.
GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
GO; GO:0008481; F:sphinganine kinase activity; IEA:UniProtKB-EC.
GO; GO:0019722; P:calcium-mediated signaling; IMP:SGD.
GO; GO:0006665; P:sphingolipid metabolic process; IDA:SGD.
Gene3D; 3.40.50.10330; -; 1.
InterPro; IPR017438; ATP-NAD_kinase_N.
InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
Pfam; PF00781; DAGK_cat; 1.
SMART; SM00046; DAGKc; 1.
SUPFAM; SSF111331; SSF111331; 1.
PROSITE; PS50146; DAGK; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Endoplasmic reticulum;
Endosome; Golgi apparatus; Isopeptide bond; Kinase; Lipid metabolism;
Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
Reference proteome; Sphingolipid metabolism; Transferase;
Ubl conjugation.
CHAIN 1 624 Sphingoid long chain base kinase 4.
/FTId=PRO_0000255956.
DOMAIN 224 363 DAGKc. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
NP_BIND 234 236 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
NP_BIND 324 326 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
NP_BIND 589 591 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
REGION 291 294 Substrate binding. {ECO:0000250}.
ACT_SITE 293 293 Proton donor/acceptor. {ECO:0000250}.
BINDING 266 266 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
BINDING 298 298 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
BINDING 392 392 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
BINDING 398 398 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 451 451 Phosphoserine; by PHO85.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:15598647}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 455 455 Phosphoserine; by PHO85.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:15598647}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
LIPID 43 43 S-palmitoyl cysteine.
{ECO:0000269|PubMed:16227572}.
LIPID 46 46 S-palmitoyl cysteine.
{ECO:0000269|PubMed:16227572}.
CROSSLNK 148 148 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
SEQUENCE 624 AA; 69639 MW; E033A3BAC604D4BB CRC64;
MVVQKKLRAI LTDEGVLIKS QSHHMFNKHG QLRSGDSLSL LSCLSCLDDG TLSSDGGSFD
EDDSLELLPL NTTIPFNRIL NAKYVNVGQK GFNNGKISSN PFQTENLSSS SENDDVENHS
LSNDKAPVSE SQSFPKKDKW DTKTNTVKVS PDDSQDNSPS LGIKDNQQLI ELTFAVPKGH
DVIPQKLTLL IDHVSRKSRA NTGEENISSG TVEEILEKSY ENSKRNRSIL VIINPHGGKG
TAKNLFLTKA RPILVESGCK IEIAYTKYAR HAIDIAKDLD ISKYDTIACA SGDGIPYEVI
NGLYRRPDRV DAFNKLAVTQ LPCGSGNAMS ISCHWTNNPS YAALCLVKSI ETRIDLMCCS
QPSYMNEWPR LSFLSQTYGV IAESDINTEF IRWMGPVRFN LGVAFNIIQG KKYPCEVFVK
YAAKSKKELK VHFLENKDKN KGCLTFEPNP SPNSSPDLLS KNNINNSTKD ELSPNFLNED
NFKLKYPMTE PVPRDWEKMD SELTDNLTIF YTGKMPYIAK DTKFFPAALP ADGTIDLVIT
DARIPVTRMT PILLSLDKGS HVLEPEVIHS KILAYKIIPK VESGLFSVDG EKFPLEPLQV
EIMPMLCKTL LRNGRYIDTE FESM


Related products :

Catalog number Product name Quantity
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
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,
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
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
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
E1358m ELISA kit Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
U1358m CLIA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
EIAAB24782 B55,GCK family kinase MiNK,Homo sapiens,Human,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 prote
E1358h ELISA kit Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
E1358h ELISA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
U1358h CLIA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
18-662-20090 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
15-288-21068 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.05 mg
18-662-20091 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
18-662-20092 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
15-288-21068 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 mg
18-785-210404 SEK1_MKK4 (Phospho-Ser80) - EC 2.7.12.2; MAP kinase kinase 4; JNK-activating kinase 1; c-Jun N-terminal kinase kinase 1; JNKK; SAPK_ERK kinase 1; SEK1 Polyclonal 0.1 mg
18-785-210403 SEK1_MKK4 (Phospho-Thr261) - EC 2.7.12.2; MAP kinase kinase 4; JNK-activating kinase 1; c-Jun N-terminal kinase kinase 1; JNKK; SAPK_ERK kinase 1; SEK1 Polyclonal 0.05 mg
18-785-210403 SEK1_MKK4 (Phospho-Thr261) - EC 2.7.12.2; MAP kinase kinase 4; JNK-activating kinase 1; c-Jun N-terminal kinase kinase 1; JNKK; SAPK_ERK kinase 1; SEK1 Polyclonal 0.1 mg
10-782-55047 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.02 mg
10-782-55048 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.05 mg
18-785-210404 SEK1_MKK4 (Phospho-Ser80) - EC 2.7.12.2; MAP kinase kinase 4; JNK-activating kinase 1; c-Jun N-terminal kinase kinase 1; JNKK; SAPK_ERK kinase 1; SEK1 Polyclonal 0.05 mg

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1653: Galactose metabolism
WP1681: Pantothenate and CoA biosynthesis
WP1701: Starch and sucrose metabolism
WP1703: Streptomycin biosynthesis
WP1844: MAP kinase cascade
WP1946: Cori Cycle
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP253: Glycolysis
WP32: Translation Factors
WP1996: Linoleate Biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1002: Electron Transport Chain
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1339: Electron Transport Chain
WP1502: Mitochondrial biogenesis
WP1614: 1- and 2-Methylnaphthalene degradation
WP1625: Base excision repair
WP1626: Benzoate degradation via CoA ligation
WP1633: Bisphenol A degradation

Related Genes :
[LCB4 YOR171C O3615] Sphingoid long chain base kinase 4 (LCB kinase 4) (EC 2.7.1.91) (Sphinganine kinase 4)
[LCB5 YLR260W] Sphingoid long chain base kinase 5 (LCB kinase 5) (EC 2.7.1.91) (Sphinganine kinase 5)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[SPTLC2 KIAA0526 LCB2] Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)
[SPHK1 SPHK SPK] Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91)
[LCB1 EMB2779 FBR11 At4g36480 AP22 C7A10.880] Long chain base biosynthesis protein 1 (AtLCB1) (EC 2.3.1.50) (Protein EMBRYO DEFECTIVE 2779) (Protein FUMONISIN B1 RESISTANT 11)
[Sphk1] Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91)
[LCB2a LCB2 At5g23670 MQM1.6] Long chain base biosynthesis protein 2a (AtLCB2a) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (AtLCB2)
[Sphk1] Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91)
[Sptlc2 Lcb2] Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)
[SBH2 At1g14290 F14L17.4 F14L17.5] Sphinganine C4-monooxygenase 2 (EC 1.14.18.5) (Sphingoid C4-hydroxylase 2) (Sphingoid base hydroxylase 2)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[SBH1 At1g69640 F24J1.22 T6C23.16] Sphinganine C4-monooxygenase 1 (EC 1.14.18.5) (Sphingoid C4-hydroxylase 1) (Sphingoid base hydroxylase 1)
[SPTLC3 C20orf38 SPTLC2L] Serine palmitoyltransferase 3 (EC 2.3.1.50) (Long chain base biosynthesis protein 2b) (LCB2b) (Long chain base biosynthesis protein 3) (LCB 3) (Serine-palmitoyl-CoA transferase 3) (SPT 3)
[zak2 DpyK4 pyk4 DDB_G0276187] Dual specificity protein kinase zak2 (EC 2.7.12.1) (Tyrosine-protein kinase 4) (Zaphod K Kinase 2) (Zaphod kinase 2)
[SLD1 At3g61580 F2A19.180] Delta(8)-fatty-acid desaturase 1 (EC 1.14.19.29) (Delta(8)-sphingolipid desaturase 1) (Sphingoid long-chain base desaturase 1) (Sphingoid LCB desaturase 1) (Sphingolipid 8-(E/Z)-desaturase 1)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[SCS7 FAH1 YMR272C YM8156.14C] Ceramide very long chain fatty acid hydroxylase SCS7 (Ceramide VLCFA hydroxylase SCS7) (4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase SCS7) (EC 1.14.18.6) (Dihydroceramide fatty acyl 2-hydroxylase SCS7) (EC 1.14.18.7) (Sphingolipid alpha-hydroxylase) (Suppressor of calcium sensitivity 7)
[SPTLC1 LCB1] Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
[PIK3CA] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[TOR2 DRR2 TSC14 YKL203C] Serine/threonine-protein kinase TOR2 (EC 2.7.1.67) (EC 2.7.11.1) (Dominant rapamycin resistance protein 2) (Phosphatidylinositol 4-kinase TOR2) (PI4-kinase TOR2) (PI4K TOR2) (PtdIns-4-kinase TOR2) (Target of rapamycin kinase 2) (Temperature-sensitive CSG2 suppressor protein 14)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Pik3cg Pi3kg1] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K)
[Sptlc1 Lcb1] Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
[SLD2 At2g46210 T3F17.14] Delta(8)-fatty-acid desaturase 2 (EC 1.14.19.29) (Delta(8)-sphingolipid desaturase 2) (Sphingoid long-chain base desaturase 2) (Sphingoid LCB desaturase 2) (Sphingolipid 8-(E/Z)-desaturase 2)
[MPK4 At4g01370 F2N1.1 F2N1_2-t] Mitogen-activated protein kinase 4 (AtMPK4) (MAP kinase 4) (EC 2.7.11.24)
[PHO85 SSG3 YPL031C P7102.18A] Cyclin-dependent protein kinase PHO85 (EC 2.7.11.22) (Negative regulator of the PHO system) (Serine/threonine-protein kinase PHO85)
[LCB1 END8 TSC2 YMR296C] Serine palmitoyltransferase 1 (SPT 1) (SPT1) (EC 2.3.1.50) (Long chain base biosynthesis protein 1)

Bibliography :
?>