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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.
12-AUG-2020, entry version 211.
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";
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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; DB01017; Minocycline.
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; 520 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.
GeneTree; ENSGT00940000156189; -.
InParanoid; P53778; -.
KO; K04441; -.
OMA; PGRDYGH; -.
OrthoDB; 233858at2759; -.
PhylomeDB; P53778; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
PathwayCommons; P53778; -.
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; 1 hit in 901 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 210 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


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