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MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1)

 MAPK3_MOUSE             Reviewed;         384 AA.
Q3UMW7; B0QZU7; E9QNE1; Q3T9E6; Q8K0G3;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
28-MAR-2018, entry version 119.
RecName: Full=MAP kinase-activated protein kinase 3;
Short=MAPK-activated protein kinase 3;
Short=MAPKAP kinase 3;
Short=MAPKAP-K3;
Short=MAPKAPK-3;
Short=MK-3;
EC=2.7.11.1;
Name=Mapkapk3;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=NOD; TISSUE=Lung, and Spleen;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Salivary gland;
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).
[5]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT
THR-203.
PubMed=17030606; DOI=10.1128/MCB.01456-06;
Ronkina N., Kotlyarov A., Dittrich-Breiholz O., Kracht M., Hitti E.,
Milarski K., Askew R., Marusic S., Lin L.L., Gaestel M., Telliez J.B.;
"The mitogen-activated protein kinase (MAPK)-activated protein kinases
MK2 and MK3 cooperate in stimulation of tumor necrosis factor
biosynthesis and stabilization of p38 MAPK.";
Mol. Cell. Biol. 27:170-181(2007).
[6]
FUNCTION IN PHOSPHORYLATION OF RPS6KA3.
PubMed=17906627; DOI=10.1038/ni1517;
Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.;
"The MAPK-activated kinase Rsk controls an acute Toll-like receptor
signaling response in dendritic cells and is activated through two
distinct pathways.";
Nat. Immunol. 8:1227-1235(2007).
[7]
ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION,
PHOSPHORYLATION AT THR-203, AND MUTAGENESIS OF THR-203.
PubMed=20570725; DOI=10.1016/j.cellsig.2010.05.019;
Moise N., Dingar D., Mamarbachi A.M., Villeneuve L.R., Farhat N.,
Gaestel M., Khairallah M., Allen B.G.;
"Characterization of a novel MK3 splice variant from murine
ventricular myocardium.";
Cell. Signal. 22:1502-1512(2010).
[8]
FUNCTION IN PHOSPHORYLATION OF KRT18 AND KRT20.
PubMed=20724476; DOI=10.1074/jbc.M110.132357;
Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,
Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate
epithelial keratins.";
J. Biol. Chem. 285:33242-33251(2010).
[9]
DISRUPTION PHENOTYPE.
PubMed=26744326; DOI=10.1093/hmg/ddv624;
Meunier I., Lenaers G., Bocquet B., Baudoin C., Piro-Megy C.,
Cubizolle A., Quiles M., Jean-Charles A., Cohen S.Y., Merle H.,
Gaudric A., Labesse G., Manes G., Pequignot M., Cazevieille C.,
Dhaenens C.M., Fichard A., Ronkina N., Arthur S.J., Gaestel M.,
Hamel C.P.;
"A dominant mutation in MAPKAPK3, an actor of p38 signaling pathway,
causes a new retinal dystrophy involving Bruch's membrane and retinal
pigment epithelium.";
Hum. Mol. Genet. 25:916-926(2016).
-!- FUNCTION: Stress-activated serine/threonine-protein kinase
involved in cytokines production, endocytosis, cell migration,
chromatin remodeling and transcriptional regulation. Following
stress, it is phosphorylated and activated by MAP kinase p38-
alpha/MAPK14, leading to phosphorylation of substrates.
Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S,
where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3,
share the same function and substrate specificity, but MAPKAPK3
kinase activity and level in protein expression are lower compared
to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1,
RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of
HSP27/HSPB1 in response to stress, leading to dissociate
HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers
and impair their chaperone activities and ability to protect
against oxidative stress effectively. Involved in inflammatory
response by regulating tumor necrosis factor (TNF) and IL6
production post-transcriptionally: acts by phosphorylating AU-rich
elements (AREs)-binding proteins, such as TTP/ZFP36, leading to
regulate the stability and translation of TNF and IL6 mRNAs.
Phosphorylation of TTP/ZFP36, a major post-transcriptional
regulator of TNF, promotes its binding to 14-3-3 proteins and
reduces its ARE mRNA affinity leading to inhibition of dependent
degradation of ARE-containing transcript. Involved in toll-like
receptor signaling pathway (TLR) in dendritic cells: required for
acute TLR-induced macropinocytosis by phosphorylating and
activating RPS6KA3. Also acts as a modulator of Polycomb-mediated
repression. {ECO:0000269|PubMed:17906627,
ECO:0000269|PubMed:20724476}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated following phosphorylation by p38-
alpha/MAPK14 following various stresses. Inhibited by ligand 5B
(2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-
dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one)
and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-
tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive
inhibitors (By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer with p38-alpha/MAPK14. The heterodimer with
p38-alpha/MAPK14 forms a stable complex: molecules are positioned
'face to face' so that the ATP-binding sites of both kinases are
at the heterodimer interface. Interacts with TCF3 and with
polycomb proteins, such as PCH2 and BMI1/PCGF4 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm.
Note=Predominantly located in the nucleus, when activated it
translocates to the cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Cytoplasm.
Note=Localizes throughout the cell. Degraded in response to
osmotic stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q3UMW7-1; Sequence=Displayed;
Name=2;
IsoId=Q3UMW7-2; Sequence=VSP_016386, VSP_016387;
Note=No experimental confirmation available.;
Name=3; Synonyms=MK3.2;
IsoId=Q3UMW7-3; Sequence=VSP_042175, VSP_042176;
-!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
Isoform 3 is expressed in skeletal muscles and heart.
{ECO:0000269|PubMed:17030606}.
-!- PTM: Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1 (By
similarity). Phosphorylated and activated by MAP kinase p38-
alpha/MAPK14 at Thr-201, Ser-251 and Thr-313. Isoform 3 is
degraded following phosphorylation at Thr-203. {ECO:0000250,
ECO:0000269|PubMed:17030606, ECO:0000269|PubMed:20570725}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are fertile and
do not exhibit behavioral phenotype. Mice do not show decreased
production of inflammatory cytokines such as TNF and IL6 upon LPS-
stimulation. Mice lacking both Mapkapk2 and Mapkapk3 show further
reduction of TNF production, compared to mice lacking only
Mapkapk2. These data suggest that Mapkapk3 may function additively
in stress-induced cytokine production. MAPKAPK3 knockdown
homozygous mice develop Bruch's membrane abnormal thickening and
thinning progressing with age (PubMed:26744326).
{ECO:0000269|PubMed:17030606, ECO:0000269|PubMed:26744326}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
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EMBL; AK087496; BAC39897.1; -; mRNA.
EMBL; AK144637; BAE25981.1; -; mRNA.
EMBL; AK151881; BAE30767.1; -; mRNA.
EMBL; AK172344; BAE42958.1; -; mRNA.
EMBL; AK172578; BAE43076.1; -; mRNA.
EMBL; AL672070; CAQ12134.1; -; Genomic_DNA.
EMBL; CH466560; EDL21175.1; -; Genomic_DNA.
EMBL; BC031467; AAH31467.1; -; mRNA.
CCDS; CCDS23487.1; -. [Q3UMW7-1]
CCDS; CCDS85722.1; -. [Q3UMW7-3]
RefSeq; NP_001303620.1; NM_001316691.1. [Q3UMW7-3]
RefSeq; NP_849238.1; NM_178907.3. [Q3UMW7-1]
RefSeq; XP_006511679.1; XM_006511616.3. [Q3UMW7-1]
UniGene; Mm.222612; -.
UniGene; Mm.445242; -.
ProteinModelPortal; Q3UMW7; -.
SMR; Q3UMW7; -.
BioGrid; 221912; 2.
STRING; 10090.ENSMUSP00000035194; -.
iPTMnet; Q3UMW7; -.
PhosphoSitePlus; Q3UMW7; -.
EPD; Q3UMW7; -.
MaxQB; Q3UMW7; -.
PaxDb; Q3UMW7; -.
PeptideAtlas; Q3UMW7; -.
PRIDE; Q3UMW7; -.
Ensembl; ENSMUST00000035194; ENSMUSP00000035194; ENSMUSG00000032577. [Q3UMW7-1]
Ensembl; ENSMUST00000192054; ENSMUSP00000141342; ENSMUSG00000032577. [Q3UMW7-3]
GeneID; 102626; -.
KEGG; mmu:102626; -.
UCSC; uc009rkx.1; mouse. [Q3UMW7-1]
UCSC; uc009rla.1; mouse. [Q3UMW7-2]
UCSC; uc012hab.1; mouse. [Q3UMW7-3]
CTD; 7867; -.
MGI; MGI:2143163; Mapkapk3.
eggNOG; KOG0604; Eukaryota.
eggNOG; ENOG410XP8F; LUCA.
GeneTree; ENSGT00900000140876; -.
HOGENOM; HOG000233031; -.
HOVERGEN; HBG106948; -.
InParanoid; Q3UMW7; -.
KO; K04444; -.
OMA; RMGQYGF; -.
OrthoDB; EOG091G14PL; -.
PhylomeDB; Q3UMW7; -.
TreeFam; TF312891; -.
Reactome; R-MMU-171007; p38MAPK events.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
PRO; PR:Q3UMW7; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032577; -.
ExpressionAtlas; Q3UMW7; baseline and differential.
Genevisible; Q3UMW7; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:UniProtKB.
Gene3D; 4.10.1170.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027442; MAPKAPK_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 384 MAP kinase-activated protein kinase 3.
/FTId=PRO_0000086294.
DOMAIN 46 306 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 52 60 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 309 345 Autoinhibitory helix. {ECO:0000250}.
REGION 347 371 p38 MAPK-binding site. {ECO:0000250}.
MOTIF 337 346 Nuclear export signal (NES).
{ECO:0000250}.
MOTIF 352 355 Bipartite nuclear localization signal 1.
{ECO:0000250}.
MOTIF 366 370 Bipartite nuclear localization signal 2.
{ECO:0000250}.
ACT_SITE 168 168 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 75 75 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q16644}.
MOD_RES 203 203 Phosphothreonine; by MAPK14.
{ECO:0000269|PubMed:17030606,
ECO:0000269|PubMed:20570725}.
MOD_RES 253 253 Phosphoserine; by MAPK14. {ECO:0000250}.
MOD_RES 309 309 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 315 315 Phosphothreonine; by MAPK14.
{ECO:0000250}.
VAR_SEQ 212 249 APEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTG ->
GESFACGLHPHCCRML (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016386.
VAR_SEQ 238 266 LCGFPPFYSNTGQAISPGMKRRIRLGQYS -> NPWWSHRP
HSTQPECSRKTKITGMTSRKR (in isoform 3).
{ECO:0000305}.
/FTId=VSP_042175.
VAR_SEQ 250 384 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016387.
VAR_SEQ 267 384 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_042176.
MUTAGEN 203 203 T->A: Prevents degradation of isoform 3.
{ECO:0000269|PubMed:20570725}.
CONFLICT 216 216 L -> P (in Ref. 1; BAE25981).
{ECO:0000305}.
SEQUENCE 384 AA; 43293 MW; 7DDE2C8E01BBD244 CRC64;
MDGETAGEKG SLVPPPGALG GSALGGAPAP GVRREPKKYA VTDDYQLSKQ VLGLGVNGKV
LECYHRRSGQ KCALKLLYDS PKARQEVDHH WQASGGPHIV RILDVYENMH HGKRCLLIVM
ECMEGGELFS RIQERGDQAF TEREAAEIMR DIGTAIQFLH SRNIAHRDVK PENLLYTSKE
KDAVLKLTDF GFAKETTQNA LQTPCYTPYY VAPEVLGPEK YDKSCDMWSL GVIMYILLCG
FPPFYSNTGQ AISPGMKRRI RLGQYSFPNP EWLDVSEDAK QLIRLLLKTD PTERLTIMQF
MNHPWINQSM VVPQTPLYTA RVLQEDKDHW DDVKEEMTSA LATMRVDYDQ VKIKDLKTSN
NRLLNKRRKK QAGSSSASQG CNNQ


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10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.01 mg
10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.005 mg
10-288-22349F MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK 0.1 mg
10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.001 mg
10-782-55070 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.02 mg
18-003-42985 MAP kinase-activated protein kinase 2 - EC 2.7.11.1; MAPK-activated protein kinase 2; MAPKAP kinase 2; MAPKAPK-2; MK2 Polyclonal 0.1 mg Protein A


 

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