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Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif kinase ZAK) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)

 M3K20_MOUSE             Reviewed;         802 AA.
Q9ESL4; Q3V1X8; Q8BR73; Q9ESL3;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
30-AUG-2017, entry version 146.
RecName: Full=Mitogen-activated protein kinase kinase kinase 20;
EC=2.7.11.25;
AltName: Full=Human cervical cancer suppressor gene 4 protein;
Short=HCCS-4;
AltName: Full=Leucine zipper- and sterile alpha motif kinase ZAK;
AltName: Full=Leucine zipper- and sterile alpha motif-containing kinase;
AltName: Full=MLK-like mitogen-activated protein triple kinase;
AltName: Full=Mitogen-activated protein kinase kinase kinase MLT;
AltName: Full=Mixed lineage kinase-related kinase;
Short=MLK-related kinase;
Short=MRK;
AltName: Full=Sterile alpha motif- and leucine zipper-containing kinase AZK;
Name=Map3k20 {ECO:0000312|MGI:MGI:2443258}; Synonyms=Mltk, Zak;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:BAB16442.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AUTOPHOSPHORYLATION, HOMODIMERIZATION, AND MUTAGENESIS OF
LYS-45.
TISSUE=Heart {ECO:0000269|PubMed:11042189};
PubMed=11042189; DOI=10.1074/jbc.M008595200;
Gotoh I., Adachi M., Nishida E.;
"Identification and characterization of a novel MAP kinase kinase
kinase, MLTK.";
J. Biol. Chem. 276:4276-4286(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH23718.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N {ECO:0000312|EMBL:AAH23718.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH23718.1};
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).
[4]
PROTEIN SEQUENCE OF 225-233, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; SER-638; SER-649
AND SER-650, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND
SER-453 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, 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).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=26755636; DOI=10.1101/gr.199430.115;
Spielmann M., Kakar N., Tayebi N., Leettola C., Nuernberg G.,
Sowada N., Lupianez D.G., Harabula I., Floettmann R., Horn D.,
Chan W.L., Wittler L., Yilmaz R., Altmueller J., Thiele H.,
van Bokhoven H., Schwartz C.E., Nuernberg P., Bowie J.U., Ahmad J.,
Kubisch C., Mundlos S., Borck G.;
"Exome sequencing and CRISPR/Cas genome editing identify mutations of
ZAK as a cause of limb defects in humans and mice.";
Genome Res. 26:183-191(2016).
-!- FUNCTION: Stress-activated component of a protein kinase signal
transduction cascade. Regulates the JNK and p38 pathways
(PubMed:11042189). Part of a signaling cascade that begins with
the activation of the adrenergic receptor ADRA1B and leads to the
activation of MAPK14 (By similarity). Pro-apoptotic. Role in
regulation of S and G2 cell cycle checkpoint by direct
phosphorylation of CHEK2 (By similarity). Involved in limb
development (PubMed:26755636). {ECO:0000250|UniProtKB:Q9NYL2,
ECO:0000269|PubMed:11042189, ECO:0000269|PubMed:26755636}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11042189}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11042189};
-!- ENZYME REGULATION: Activated by phosphorylation by PKN1 and
autophosphorylation on Thr-161 and Ser-165.
{ECO:0000250|UniProtKB:Q9NYL2}.
-!- SUBUNIT: Homodimer (PubMed:11042189). Interacts with PKN1 and
ZNF33A. Component of a signaling complex containing at least
AKAP13, PKN1, MAPK14, MAP3K20 and MAP2K3. Within this complex,
AKAP13 interacts directly with PKN1, which in turn recruits
MAPK14, MAP2K3 and MAP3K20. {ECO:0000250|UniProtKB:Q9NYL2,
ECO:0000269|PubMed:11042189}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11042189}.
Nucleus {ECO:0000269|PubMed:11042189}. Note=Appears to shuttle
between nucleus and cytoplasm. {ECO:0000269|PubMed:11042189}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:11042189}; Synonyms=Alpha;
IsoId=Q9ESL4-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:11042189}; Synonyms=Beta;
IsoId=Q9ESL4-2; Sequence=VSP_051745, VSP_051746;
Note=Contains a phosphoserine at position 434. Contains a
phosphoserine at position 453. {ECO:0000244|PubMed:21183079};
Name=3 {ECO:0000305};
IsoId=Q9ESL4-3; Sequence=VSP_051747, VSP_051748;
Note=No experimental confirmation available. {ECO:0000305};
-!- DEVELOPMENTAL STAGE: Mainly expressed in heart and developing
limbs. {ECO:0000269|PubMed:26755636}.
-!- DISRUPTION PHENOTYPE: Knockout results in fully penetrant
lethality at E9.5 duse to severe cardiac edema and growth
retardation. Embryos show polydactyly of the feet.
{ECO:0000269|PubMed:26755636}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
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EMBL; AB049731; BAB16442.1; -; mRNA.
EMBL; AB049732; BAB16443.1; -; mRNA.
EMBL; AK045444; BAC32371.1; -; mRNA.
EMBL; AK132186; BAE21021.1; -; mRNA.
EMBL; BC023718; AAH23718.1; -; mRNA.
CCDS; CCDS38143.1; -. [Q9ESL4-1]
CCDS; CCDS50605.1; -. [Q9ESL4-2]
RefSeq; NP_001158263.1; NM_001164791.1. [Q9ESL4-2]
RefSeq; NP_075544.1; NM_023057.5. [Q9ESL4-1]
RefSeq; NP_835185.2; NM_178084.4. [Q9ESL4-3]
RefSeq; XP_006500060.1; XM_006499997.2. [Q9ESL4-1]
UniGene; Mm.304143; -.
UniGene; Mm.314618; -.
ProteinModelPortal; Q9ESL4; -.
SMR; Q9ESL4; -.
IntAct; Q9ESL4; 1.
MINT; MINT-4129310; -.
STRING; 10090.ENSMUSP00000088334; -.
iPTMnet; Q9ESL4; -.
PhosphoSitePlus; Q9ESL4; -.
PaxDb; Q9ESL4; -.
PeptideAtlas; Q9ESL4; -.
PRIDE; Q9ESL4; -.
Ensembl; ENSMUST00000090824; ENSMUSP00000088334; ENSMUSG00000004085. [Q9ESL4-1]
Ensembl; ENSMUST00000135469; ENSMUSP00000118983; ENSMUSG00000004085. [Q9ESL4-2]
GeneID; 65964; -.
KEGG; mmu:65964; -.
UCSC; uc008kbs.2; mouse. [Q9ESL4-3]
UCSC; uc008kbv.2; mouse. [Q9ESL4-1]
CTD; 51776; -.
MGI; MGI:2443258; Map3k20.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118807; -.
HOGENOM; HOG000231813; -.
HOVERGEN; HBG080445; -.
InParanoid; Q9ESL4; -.
KO; K04424; -.
OMA; QWRCEIE; -.
OrthoDB; EOG091G037E; -.
PhylomeDB; Q9ESL4; -.
TreeFam; TF106505; -.
PRO; PR:Q9ESL4; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000004085; -.
CleanEx; MM_B230120H23RIK; -.
ExpressionAtlas; Q9ESL4; baseline and differential.
Genevisible; Q9ESL4; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0007257; P:activation of JUN kinase activity; ISO:MGI.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0000075; P:cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
GO; GO:0000077; P:DNA damage checkpoint; ISO:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0009314; P:response to radiation; ISO:MGI.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032938; MLTK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR23257:SF591; PTHR23257:SF591; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00220; S_TKc; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Cell cycle;
Complete proteome; Cytoplasm; Direct protein sequencing; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9NYL2}.
CHAIN 2 802 Mitogen-activated protein kinase kinase
kinase 20.
/FTId=PRO_0000086339.
DOMAIN 16 277 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 339 410 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 22 30 ATP. {ECO:0000250|UniProtKB:P80192,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 287 308 Leucine-zipper.
ACT_SITE 133 133 Proton acceptor.
{ECO:0000250|UniProtKB:P80192,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 45 45 ATP. {ECO:0000250|UniProtKB:Q9NYL2,
ECO:0000255|PROSITE-ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 161 161 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 165 165 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 599 599 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 628 628 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 638 638 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 685 685 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
MOD_RES 733 733 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYL2}.
VAR_SEQ 285 289 CEIEA -> WVAPA (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_051747.
VAR_SEQ 290 802 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_051748.
VAR_SEQ 332 454 PSFEIGAWTEDDVYFWVQQLVRKGESSVEMSGYASLFKENN
ITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYLN
LFHFPPLIKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQD
-> LPLSARMSEESYFESKTEESNSAEMSCQITAASNGEGH
GMNPGLQAMMLMGFGDVFSMNKAGAVLHSGMQINMQAKQNS
SKTTCKRRGKKVNMALGFSDFDLSEGDDDDHDGDDAENDVD
NSE (in isoform 2).
{ECO:0000303|PubMed:11042189}.
/FTId=VSP_051745.
VAR_SEQ 455 802 Missing (in isoform 2).
{ECO:0000303|PubMed:11042189}.
/FTId=VSP_051746.
MUTAGEN 45 45 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:11042189}.
CONFLICT 171 171 P -> Q (in Ref. 2; BAC32371).
{ECO:0000305}.
SEQUENCE 802 AA; 91720 MW; D431DF8F312A43CC CRC64;
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI EKEAEILSVL
SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE EMDMEHIMTW ATDVAKGMHY
LHMEAPVKVI HRDLKSRNVV IAADGVLKIC DFGASRFHNH TTHMSLVGTF PWMAPEVIQS
LPVSETCDTY SYGVVLWEML TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH
QCWEADAKKR PSFKQIISIL ESMSNDTNLP DQCNSFLHNK AEWRCEIEAT LERLKKLERD
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYFWVQQ LVRKGESSVE
MSGYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF KSAIEKLTHD YLNLFHFPPL
IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT GPQDCKWKMY MEMDGDEVAI TYIKDVTFNT
SLPDAEILKM TKPPFVMEKW IVGIAEDQTV ECTVTYENDV RTPKLTKHVH SIQWDRTKPQ
DEVKAVQLAI QTLFSSSEGN PGSRSDSSAD CQWLDTLRMR QIASHTSLQR SQSNPILGSP
FFPYFANQDS YAAAVRRTQT PVKYQQITPS INPSRSSSPT QYGLSRNFSS LNLSSRDSGF
SSLNDSSSER GRYSDRSRNK YYRGSVSLNS SPKGRYGGKS QHSTPSRERY SGKFYRLPQS
ALNTHQSPDF KRSPNDHDRR VPRTIPGMPL HPETASKAGE EESRVSEGGW TKVEYRKKTH
RQLSAKTSKE RTRGNYRGRR NF


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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
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
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
18-662-20091 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
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
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 0.02 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 0.05 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


 

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