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

Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)

 MK12_HUMAN              Reviewed;         367 AA.
P53778; Q14260; Q6IC53; Q99588; Q99672;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
17-JUN-2020, entry version 210.
RecName: Full=Mitogen-activated protein kinase 12;
Short=MAP kinase 12;
Short=MAPK 12;
EC=2.7.11.24 {ECO:0000269|PubMed:10212242};
AltName: Full=Extracellular signal-regulated kinase 6;
Short=ERK-6;
AltName: Full=Mitogen-activated protein kinase p38 gamma;
Short=MAP kinase p38 gamma;
AltName: Full=Stress-activated protein kinase 3;
Name=MAPK12; Synonyms=ERK6, SAPK3;
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 1), FUNCTION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF TYR-185.
TISSUE=Skeletal muscle;
PubMed=8633070; DOI=10.1073/pnas.93.9.4355;
Lechner C., Zahalka M.A., Giot J.-F., Moeller N.P.H., Ullrich A.;
"ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 93:4355-4359(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=9169156; DOI=10.1006/geno.1997.4633;
Goedert M., Hasegawa J., Craxton M., Leversha M.A., Clegg S.;
"Assignment of the human stress-activated protein kinase-3 gene (SAPK3) to
chromosome 22q13.3 by fluorescence in situ hybridization.";
Genomics 41:501-502(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8920915; DOI=10.1006/bbrc.1996.1662;
Li Z., Jiang Y., Ulevitch R.J., Han J.;
"The primary structure of p38 gamma: a new member of p38 group of MAP
kinases.";
Biochem. Biophys. Res. Commun. 228:334-340(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-103.
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[7]
FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, AND ACTIVITY REGULATION.
PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
Enslen H., Raingeaud J., Davis R.J.;
"Selective activation of p38 mitogen-activated protein (MAP) kinase
isoforms by the MAP kinase kinases MKK3 and MKK6.";
J. Biol. Chem. 273:1741-1748(1998).
[8]
INTERACTION WITH SNTA1, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
AND CATALYTIC ACTIVITY.
PubMed=10212242; DOI=10.1074/jbc.274.18.12626;
Hasegawa M., Cuenda A., Spillantini M.G., Thomas G.M., Buee-Scherrer V.,
Cohen P., Goedert M.;
"Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-
syntrophin. A mechanism for specific substrate recognition.";
J. Biol. Chem. 274:12626-12631(1999).
[9]
PHOSPHORYLATION BY MAP2K6/MKK6.
PubMed=11010976; DOI=10.1074/jbc.m007835200;
Alonso G., Ambrosino C., Jones M., Nebreda A.R.;
"Differential activation of p38 mitogen-activated protein kinase isoforms
depending on signal strength.";
J. Biol. Chem. 275:40641-40648(2000).
[10]
FUNCTION IN REGULATION OF THE G2 CHECKPOINT.
PubMed=10848581; DOI=10.1128/mcb.20.13.4543-4552.2000;
Wang X., McGowan C.H., Zhao M., He L., Downey J.S., Fearns C., Wang Y.,
Huang S., Han J.;
"Involvement of the MKK6-p38gamma cascade in gamma-radiation-induced cell
cycle arrest.";
Mol. Cell. Biol. 20:4543-4552(2000).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=11991731; DOI=10.1006/jmcc.2001.1523;
Court N.W., dos Remedios C.G., Cordell J., Bogoyevitch M.A.;
"Cardiac expression and subcellular localization of the p38 mitogen-
activated protein kinase member, stress-activated protein kinase-3
(SAPK3).";
J. Mol. Cell. Cardiol. 34:413-426(2002).
[12]
MUTAGENESIS, SUBCELLULAR LOCATION, AND INTERACTION WITH SH3BP5.
PubMed=12167088; DOI=10.1042/bj20020553;
Wiltshire C., Matsushita M., Tsukada S., Gillespie D.A., May G.H.;
"A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5),
associates with mitochondria.";
Biochem. J. 367:577-585(2002).
[13]
FUNCTION.
PubMed=14592936; DOI=10.1152/ajpregu.00563.2003;
Ho R.C., Alcazar O., Fujii N., Hirshman M.F., Goodyear L.J.;
"p38gamma MAPK regulation of glucose transporter expression and glucose
uptake in L6 myotubes and mouse skeletal muscle.";
Am. J. Physiol. 286:R342-R349(2004).
[14]
MUTAGENESIS OF ASP-179 AND PHE-330.
PubMed=15284239; DOI=10.1074/jbc.m404595200;
Diskin R., Askari N., Capone R., Engelberg D., Livnah O.;
"Active mutants of the human p38alpha mitogen-activated protein kinase.";
J. Biol. Chem. 279:47040-47049(2004).
[15]
FUNCTION, INDUCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
UBIQUITINATION.
PubMed=17724032; DOI=10.1074/jbc.m703857200;
Qi X., Pohl N.M., Loesch M., Hou S., Li R., Qin J.Z., Cuenda A., Chen G.;
"p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-
proteasome pathways in regulating Ras transformation and stress response.";
J. Biol. Chem. 282:31398-31408(2007).
[16]
FUNCTION IN PHOSPHORYLATION OF DLG1.
PubMed=20605917; DOI=10.1242/jcs.066514;
Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A.,
Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A.;
"p38gamma regulates interaction of nuclear PSF and RNA with the tumour-
suppressor hDlg in response to osmotic shock.";
J. Cell Sci. 123:2596-2604(2010).
[17]
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).
[18]
FUNCTION.
PubMed=21172807; DOI=10.1242/jcs.068254;
Kukkonen-Macchi A., Sicora O., Kaczynska K., Oetken-Lindholm C.,
Pouwels J., Laine L., Kallio M.J.;
"Loss of p38gamma MAPK induces pleiotropic mitotic defects and massive cell
death.";
J. Cell Sci. 124:216-227(2011).
[19]
INVOLVEMENT IN CANCER.
PubMed=21532888; DOI=10.1593/neo.101748;
Meng F., Zhang H., Liu G., Kreike B., Chen W., Sethi S., Miller F.R.,
Wu G.;
"p38gamma mitogen-activated protein kinase contributes to oncogenic
properties maintenance and resistance to poly (ADP-ribose)-polymerase-1
inhibition in breast cancer.";
Neoplasia 13:472-482(2011).
[20]
REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION.
PubMed=20626350; DOI=10.1042/bj20100323;
Cuadrado A., Nebreda A.R.;
"Mechanisms and functions of p38 MAPK signalling.";
Biochem. J. 429:403-417(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[22]
INTERACTION WITH PTPN4.
PubMed=27246854; DOI=10.1074/jbc.m115.707208;
Maisonneuve P., Caillet-Saguy C., Vaney M.C., Bibi-Zainab E., Sawyer K.,
Raynal B., Haouz A., Delepierre M., Lafon M., Cordier F., Wolff N.;
"Molecular Basis of the Interaction of the Human Protein Tyrosine
Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein
Kinase p38gamma.";
J. Biol. Chem. 291:16699-16708(2016).
[23]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), COFACTOR, AND SUBUNIT.
PubMed=10508788; DOI=10.1016/s0969-2126(99)80173-7;
Bellon S., Fitzgibbon M.J., Fox T., Hsiao H.M., Wilson K.P.;
"The structure of phosphorylated p38gamma is monomeric and reveals a
conserved activation-loop conformation.";
Structure 7:1057-1065(1999).
[24]
VARIANTS [LARGE SCALE ANALYSIS] MET-103 AND ASN-230.
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 kinase which acts as an essential component
of the MAP kinase signal transduction pathway. MAPK12 is one of the
four p38 MAPKs which play an important role in the cascades of cellular
responses evoked by extracellular stimuli such as proinflammatory
cytokines or physical stress leading to direct activation of
transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs
phosphorylate a broad range of proteins and it has been estimated that
they may have approximately 200 to 300 substrates each. Some of the
targets are downstream kinases such as MAPKAPK2, which are activated
through phosphorylation and further phosphorylate additional targets.
Plays a role in myoblast differentiation and also in the down-
regulation of cyclin D1 in response to hypoxia in adrenal cells
suggesting MAPK12 may inhibit cell proliferation while promoting
differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12
in the cell nucleus increases its association with nuclear DLG1,
thereby causing dissociation of DLG1-SFPQ complexes. This function is
independent of its catalytic activity and could affect mRNA processing
and/or gene transcription to aid cell adaptation to osmolarity changes
in the environment. Regulates UV-induced checkpoint signaling and
repair of UV-induced DNA damage and G2 arrest after gamma-radiation
exposure. MAPK12 is involved in the regulation of SLC2A1 expression and
basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4
expression and contraction-mediated glucose uptake in adult skeletal
muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and
inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is
required for the normal kinetochore localization of PLK1, prevents
chromosomal instability and supports mitotic cell viability. MAPK12-
signaling is also positively regulating the expansion of transient
amplifying myogenic precursor cells during muscle growth and
regeneration. {ECO:0000269|PubMed:10848581,
ECO:0000269|PubMed:14592936, ECO:0000269|PubMed:17724032,
ECO:0000269|PubMed:20605917, ECO:0000269|PubMed:21172807,
ECO:0000269|PubMed:8633070, ECO:0000269|PubMed:9430721}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
Evidence={ECO:0000269|PubMed:10212242};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24; Evidence={ECO:0000269|PubMed:10212242};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10508788};
Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:10508788};
-!- ACTIVITY REGULATION: Activated by phosphorylation on threonine and
tyrosine. MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the
activation of MAPK12 induced by environmental stress, whereas
MAP2K6/MKK6 is the major MAPK12 activator in response to TNF-alpha.
{ECO:0000269|PubMed:10212242, ECO:0000269|PubMed:9430721}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=37 uM for ATP {ECO:0000269|PubMed:10212242};
KM=313 uM for EGFR substrate peptide {ECO:0000269|PubMed:10212242};
KM=254 uM for GST-ATF2 {ECO:0000269|PubMed:10212242};
-!- SUBUNIT: Monomer. Interacts with the PDZ domain of the syntrophin
SNTA1. Interacts with SH3BP5. Interacts with LIN7C, SCRIB and SYNJ2BP
(By similarity). Interacts with PTPN4; this interaction induces the
activation of PTPN4 phosphatase activity. {ECO:0000250,
ECO:0000269|PubMed:27246854}.
-!- INTERACTION:
P53778; Q12959: DLG1; NbExp=2; IntAct=EBI-602406, EBI-357481;
P53778; Q16512: PKN1; NbExp=2; IntAct=EBI-602406, EBI-602382;
P53778; P29074: PTPN4; NbExp=2; IntAct=EBI-602406, EBI-710431;
P53778; Q14160: SCRIB; NbExp=6; IntAct=EBI-602406, EBI-357345;
P53778; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-602406, EBI-747107;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion.
Note=Mitochondrial when associated with SH3BP5. In skeletal muscle
colocalizes with SNTA1 at the neuromuscular junction and throughout the
sarcolemma (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P53778-1; Sequence=Displayed;
Name=2;
IsoId=P53778-2; Sequence=VSP_055224;
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart.
{ECO:0000269|PubMed:11991731, ECO:0000269|PubMed:8633070}.
-!- INDUCTION: Expression of MAPK12 is down-regulation by MAPK14
activation. {ECO:0000269|PubMed:17724032}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and
MAP2K6/MKK6, which activates the enzyme. {ECO:0000269|PubMed:11010976,
ECO:0000269|PubMed:17724032}.
-!- PTM: Ubiquitinated. Ubiquitination leads to degradation by the
proteasome pathway. {ECO:0000269|PubMed:17724032}.
-!- DISEASE: Note=MAPK is overexpressed in highly metastatic breast cancer
cell lines and its expression is preferentially associated with basal-
like and metastatic phenotypes of breast tumor samples.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. MAP kinase subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPK12ID41290ch22q13.html";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; X79483; CAA55984.1; -; mRNA.
EMBL; Y10487; CAA71511.1; -; mRNA.
EMBL; U66243; AAB40118.1; -; mRNA.
EMBL; CR456515; CAG30401.1; -; mRNA.
EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015741; AAH15741.1; -; mRNA.
CCDS; CCDS14089.1; -. [P53778-1]
CCDS; CCDS77688.1; -. [P53778-2]
PIR; JC5252; JC5252.
PIR; JC6138; JC6138.
RefSeq; NP_001290181.1; NM_001303252.2. [P53778-2]
RefSeq; NP_002960.2; NM_002969.5. [P53778-1]
PDB; 1CM8; X-ray; 2.40 A; A/B=1-367.
PDB; 4QUM; X-ray; 2.52 A; B=182-190.
PDB; 6UNA; X-ray; 2.55 A; A/B=7-367.
PDBsum; 1CM8; -.
PDBsum; 4QUM; -.
PDBsum; 6UNA; -.
SMR; P53778; -.
BioGRID; 112207; 41.
CORUM; P53778; -.
DIP; DIP-34241N; -.
IntAct; P53778; 19.
MINT; P53778; -.
STRING; 9606.ENSP00000215659; -.
BindingDB; P53778; -.
ChEMBL; CHEMBL4674; -.
DrugBank; DB05403; CEP-1347.
DrugBank; DB05157; KC706.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB02482; Phosphonothreonine.
DrugCentral; P53778; -.
GuidetoPHARMACOLOGY; 1501; -.
iPTMnet; P53778; -.
PhosphoSitePlus; P53778; -.
BioMuta; MAPK12; -.
DMDM; 2851522; -.
CPTAC; CPTAC-874; -.
CPTAC; CPTAC-875; -.
EPD; P53778; -.
jPOST; P53778; -.
MassIVE; P53778; -.
MaxQB; P53778; -.
PaxDb; P53778; -.
PeptideAtlas; P53778; -.
PRIDE; P53778; -.
ProteomicsDB; 56615; -. [P53778-1]
Antibodypedia; 14291; 514 antibodies.
DNASU; 6300; -.
Ensembl; ENST00000215659; ENSP00000215659; ENSG00000188130. [P53778-1]
Ensembl; ENST00000622558; ENSP00000479972; ENSG00000188130. [P53778-2]
GeneID; 6300; -.
KEGG; hsa:6300; -.
UCSC; uc003bkl.2; human. [P53778-1]
CTD; 6300; -.
DisGeNET; 6300; -.
EuPathDB; HostDB:ENSG00000188130.13; -.
GeneCards; MAPK12; -.
HGNC; HGNC:6874; MAPK12.
HPA; ENSG00000188130; Tissue enriched (skeletal).
MIM; 602399; gene.
neXtProt; NX_P53778; -.
OpenTargets; ENSG00000188130; -.
PharmGKB; PA30619; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00940000156189; -.
InParanoid; P53778; -.
KO; K04441; -.
OMA; PGRDYGH; -.
OrthoDB; 233858at2759; -.
PhylomeDB; P53778; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-376172; DSCAM interactions.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-525793; Myogenesis.
SignaLink; P53778; -.
SIGNOR; P53778; -.
BioGRID-ORCS; 6300; 0 hits in 815 CRISPR screens.
ChiTaRS; MAPK12; human.
EvolutionaryTrace; P53778; -.
GeneWiki; MAPK12; -.
GenomeRNAi; 6300; -.
Pharos; P53778; Tchem.
PRO; PR:P53778; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; P53778; protein.
Bgee; ENSG00000188130; Expressed in gastrocnemius and 196 other tissues.
ExpressionAtlas; P53778; baseline and differential.
Genevisible; P53778; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; TAS:ProtInc.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
GO; GO:0045445; P:myoblast differentiation; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0010952; P:positive regulation of peptidase activity; NAS:ParkinsonsUK-UCL.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd07880; STKc_p38gamma; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38-like.
InterPro; IPR038786; p38gamma.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01773; P38MAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cytoplasm;
Kinase; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1..367
/note="Mitogen-activated protein kinase 12"
/id="PRO_0000186282"
DOMAIN 27..311
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 33..41
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 183..185
/note="TXY"
ACT_SITE 153
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 56
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 183
/note="Phosphothreonine; by MAP2K3 and MAP2K6"
/evidence="ECO:0000250|UniProtKB:Q63538"
MOD_RES 185
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:23186163"
VAR_SEQ 142..151
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15461802"
/id="VSP_055224"
VARIANT 103
/note="T -> M (in dbSNP:rs34422484)"
/evidence="ECO:0000269|PubMed:15461802,
ECO:0000269|PubMed:17344846"
/id="VAR_042265"
VARIANT 230
/note="D -> N (in dbSNP:rs35396905)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042266"
VARIANT 244
/note="T -> M (in dbSNP:rs2066776)"
/id="VAR_012002"
MUTAGEN 179
/note="D->A: Emulation of the active state."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 185
/note="Y->F: Loss of activity."
/evidence="ECO:0000269|PubMed:8633070"
MUTAGEN 330
/note="F->S: No effect."
/evidence="ECO:0000269|PubMed:15284239"
CONFLICT 7
/note="A -> T (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 70
/note="R -> L (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 138
/note="L -> M (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 201..202
/note="MR -> IA (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 261
/note="Y -> N (in Ref. 3; AAB40118)"
/evidence="ECO:0000305"
CONFLICT 297..298
/note="EQ -> DI (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 300
/note="V -> L (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 305
/note="A -> F (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 307
/note="A -> S (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
CONFLICT 332..333
/note="DV -> YF (in Ref. 1; CAA55984)"
/evidence="ECO:0000305"
STRAND 11..15
/evidence="ECO:0000244|PDB:6UNA"
STRAND 17..21
/evidence="ECO:0000244|PDB:1CM8"
STRAND 24..32
/evidence="ECO:0000244|PDB:1CM8"
STRAND 41..46
/evidence="ECO:0000244|PDB:1CM8"
TURN 47..49
/evidence="ECO:0000244|PDB:1CM8"
STRAND 52..57
/evidence="ECO:0000244|PDB:1CM8"
HELIX 65..80
/evidence="ECO:0000244|PDB:1CM8"
STRAND 90..93
/evidence="ECO:0000244|PDB:1CM8"
TURN 99..101
/evidence="ECO:0000244|PDB:1CM8"
STRAND 106..110
/evidence="ECO:0000244|PDB:1CM8"
STRAND 113..115
/evidence="ECO:0000244|PDB:1CM8"
HELIX 116..122
/evidence="ECO:0000244|PDB:1CM8"
HELIX 127..146
/evidence="ECO:0000244|PDB:1CM8"
HELIX 156..158
/evidence="ECO:0000244|PDB:1CM8"
STRAND 159..161
/evidence="ECO:0000244|PDB:1CM8"
STRAND 167..169
/evidence="ECO:0000244|PDB:1CM8"
HELIX 189..191
/evidence="ECO:0000244|PDB:1CM8"
HELIX 195..198
/evidence="ECO:0000244|PDB:1CM8"
TURN 199..201
/evidence="ECO:0000244|PDB:1CM8"
HELIX 207..221
/evidence="ECO:0000244|PDB:1CM8"
HELIX 231..242
/evidence="ECO:0000244|PDB:1CM8"
HELIX 247..251
/evidence="ECO:0000244|PDB:1CM8"
HELIX 256..264
/evidence="ECO:0000244|PDB:1CM8"
HELIX 273..275
/evidence="ECO:0000244|PDB:1CM8"
HELIX 282..291
/evidence="ECO:0000244|PDB:1CM8"
TURN 296..298
/evidence="ECO:0000244|PDB:1CM8"
HELIX 302..307
/evidence="ECO:0000244|PDB:1CM8"
HELIX 309..311
/evidence="ECO:0000244|PDB:1CM8"
TURN 312..314
/evidence="ECO:0000244|PDB:1CM8"
HELIX 329..332
/evidence="ECO:0000244|PDB:6UNA"
HELIX 337..349
/evidence="ECO:0000244|PDB:1CM8"
SEQUENCE 367 AA; 41940 MW; EF680401D8E40610 CRC64;
MSSPPPARSG FYRQEVTKTA WEVRAVYRDL QPVGSGAYGA VCSAVDGRTG AKVAIKKLYR
PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD DFTDFYLVMP FMGTDLGKLM
KHEKLGEDRI QFLVYQMLKG LRYIHAAGII HRDLKPGNLA VNEDCELKIL DFGLARQADS
EMTGYVVTRW YRAPEVILNW MRYTQTVDIW SVGCIMAEMI TGKTLFKGSD HLDQLKEIMK
VTGTPPAEFV QRLQSDEAKN YMKGLPELEK KDFASILTNA SPLAVNLLEK MLVLDAEQRV
TAGEALAHPY FESLHDTEDE PQVQKYDDSF DDVDRTLDEW KRVTYKEVLS FKPPRQLGAR
VSKETPL


Related products :

Catalog number Product name Quantity
EIAAB24867 ERK6,ERK-6,Extracellular signal-regulated kinase 6,Homo sapiens,Human,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,MAPK12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,S
EIAAB24866 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Mouse,Mus musculus,Sapk3,
EIAAB24868 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Rat,Rattus norvegicus,Sap
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.005 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
E1206m ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
E1206r ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
E1206b ELISA kit Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
E1206m ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206r ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206h ELISA kit ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-ac 96T
E1206h ELISA ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activat 96T
U1206h CLIA ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activate 96T
18-662-20087 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 Polyclonal 0.1 ml
15-288-22768 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 Polyclonal 0.05 mg
15-288-22768 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 Polyclonal 0.1 mg
10-782-55051 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 N_A 0.05 mg
Pathways :
WP1493: Carbon assimilation C4 pathway
WP32: Translation Factors
WP1567: Glycolysis and Gluconeogenesis
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1619: Amino sugar and nucleotide sugar metabolism
WP1844: MAP kinase cascade
WP1701: Starch and sucrose metabolism
WP2292: Chemokine signaling pathway
WP1946: Cori Cycle
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP253: Glycolysis
WP1653: Galactose metabolism
WP1681: Pantothenate and CoA biosynthesis
WP2199: Seed Development
WP1703: Streptomycin biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP1673: Naphthalene and anthracene degradation
WP1678: Nucleotide excision repair
WP211: BMP signaling pathway
WP1888: Post-translational protein modification
WP731: Sterol regulatory element binding protein related
WP1438: Influenza A virus infection
WP1689: Porphyrin and chlorophyll metabolism
WP2152: BDNF

Related Genes :
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk13 Serk4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[mapk14b mapk14] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (zp38b)
[mapk14a mapk14] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (zp38a)
[mapk14b] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (cp38b)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[p38b CG7393] Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
[mapk14a] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (cp38a)
[pmk-1 B0218.3] Mitogen-activated protein kinase pmk-1 (EC 2.7.11.24) (Stress-activated protein kinase pmk-1) (p38 MAP kinase 1)
[MAPK14 CSBP1] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a)
[pmk-3 F42G8.4] Mitogen-activated protein kinase pmk-3 (EC 2.7.11.24) (Stress-activated protein kinase pmk-3) (p38 MAP kinase 3)
[MAPKAPK5 PRAK] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk3 Erk1 Prkm3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[Mapk7 Bmk1 Erk5] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[Mapk3 Erk1 Prkm3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)

Bibliography :
No related Items