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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_RAT                Reviewed;         367 AA.
Q63538;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 155.
RecName: Full=Mitogen-activated protein kinase 12;
Short=MAP kinase 12;
Short=MAPK 12;
EC=2.7.11.24;
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=Sapk3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=8925912; DOI=10.1016/0014-5793(96)00255-4;
Mertens S., Craxton M., Goedert M.;
"SAP kinase-3, a new member of the family of mammalian stress-
activated protein kinases.";
FEBS Lett. 383:273-276(1996).
[2]
INTERACTION WITH SNTA1, FUNCTION IN PHOSPHORYLATION OF SNTA1, AND
SUBCELLULAR LOCATION.
PubMed=19135240; DOI=10.1016/j.cell.2008.11.018;
Sumara G., Formentini I., Collins S., Sumara I., Windak R.,
Bodenmiller B., Ramracheya R., Caille D., Jiang H., Platt K.A.,
Meda P., Aebersold R., Rorsman P., Ricci R.;
"Regulation of PKD by the MAPK p38delta in insulin secretion and
glucose homeostasis.";
Cell 136:235-248(2009).
[3]
FUNCTION, PHOSPHORYLATION AT THR-183 AND TYR-185, AND MUTAGENESIS OF
THR-183 AND TYR-185.
PubMed=10438538; DOI=10.1074/jbc.274.33.23570;
Conrad P.W., Rust R.T., Han J., Millhorn D.E., Beitner-Johnson D.;
"Selective activation of p38alpha and p38gamma by hypoxia. Role in
regulation of cyclin D1 by hypoxia in PC12 cells.";
J. Biol. Chem. 274:23570-23576(1999).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[5]
SUBCELLULAR LOCATION, AND INTERACTION WITH SH3BP5.
PubMed=15158451; DOI=10.1016/j.bbrc.2004.04.148;
Court N.W., Kuo I., Quigley O., Bogoyevitch M.A.;
"Phosphorylation of the mitochondrial protein Sab by stress-activated
protein kinase 3.";
Biochem. Biophys. Res. Commun. 319:130-137(2004).
[6]
INTERACTION WITH LIN7C; SCRIB AND SYNJ2BP, AND ACTIVITY REGULATION.
PubMed=15878399; DOI=10.1016/j.bbamcr.2004.11.008;
Court N.W., Ingley E., Klinken S.P., Bogoyevitch M.A.;
"Outer membrane protein 25-a mitochondrial anchor and inhibitor of
stress-activated protein kinase-3.";
Biochim. Biophys. Acta 1744:68-75(2005).
[7]
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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:10438538, ECO:0000269|PubMed:19135240}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 2 magnesium ions.;
-!- 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:15878399}.
-!- SUBUNIT: Monomer. Interacts with the PDZ domain of the syntrophin
SNTA1. Interacts with LIN7C, SCRIB, SYNJ2BP and SH3BP5.
{ECO:0000269|PubMed:15158451, ECO:0000269|PubMed:15878399,
ECO:0000269|PubMed:19135240}.
-!- INTERACTION:
Q13424:SNTA1 (xeno); NbExp=5; IntAct=EBI-783937, EBI-717191;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
Mitochondrion. Note=Mitochondrial when associated with SH3BP5. In
skeletal muscle colocalizes with SNTA1 at the neuromuscular
junction and throughout the sarcolemma.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, lung and
testes and also in the heart and thymus of both adult and neonatal
rats. {ECO:0000269|PubMed:11991731}.
-!- 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:10438538}.
-!- PTM: Ubiquitinated. Ubiquitination leads to degradation by the
proteasome pathway (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X96488; CAA65342.1; -; mRNA.
PIR; S68680; S68680.
RefSeq; NP_068514.1; NM_021746.1.
UniGene; Rn.162968; -.
ProteinModelPortal; Q63538; -.
SMR; Q63538; -.
BioGrid; 248795; 1.
DIP; DIP-37835N; -.
IntAct; Q63538; 3.
STRING; 10116.ENSRNOP00000046455; -.
iPTMnet; Q63538; -.
PhosphoSitePlus; Q63538; -.
PaxDb; Q63538; -.
PRIDE; Q63538; -.
Ensembl; ENSRNOT00000044376; ENSRNOP00000046455; ENSRNOG00000031233.
GeneID; 60352; -.
KEGG; rno:60352; -.
CTD; 6300; -.
RGD; 70975; Mapk12.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q63538; -.
KO; K04441; -.
OMA; MSSGAMD; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; Q63538; -.
TreeFam; TF105100; -.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-375170; CDO in myogenesis.
Reactome; R-RNO-376172; DSCAM interactions.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
PRO; PR:Q63538; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000031233; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0004707; F:MAP kinase activity; IDA:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase;
Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transcription; Transcription regulation; Transferase;
Ubl conjugation.
CHAIN 1 367 Mitogen-activated protein kinase 12.
/FTId=PRO_0000186284.
DOMAIN 27 311 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 33 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 183 185 TXY.
ACT_SITE 153 153 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 56 56 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 183 183 Phosphothreonine; by MAP2K3 and MAP2K6.
{ECO:0000269|PubMed:10438538}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K3 and MAP2K6.
{ECO:0000269|PubMed:10438538}.
MUTAGEN 183 183 T->A: Loss of kinase activity.
{ECO:0000269|PubMed:10438538}.
MUTAGEN 185 185 Y->A: Loss of kinase activity.
{ECO:0000269|PubMed:10438538}.
SEQUENCE 367 AA; 41985 MW; B77193D9F45E1D4E CRC64;
MSSPPPARKG FYRQEVTKTA WEVRAVYQDL QPVGSGAYGA VCSAVDSRTG NKVAIKKLYR
PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD DFTDFYLVMP FMGTDLGKLM
KHETLSEDRI QFLVYQMLKG LKYIHAAGVI HRDLKPGNLA VNEDCELKIL DFGLARQADS
EMTGYVVTRW YRAPEVILNW MRYTQTVDIW SVGCIMAEMI TGKILFKGND HLDQLKEIMK
VTGTPPPEFV QKLQSAEAKN YMEGLPELEK KDFASVLTNA SPQAVNLLEK MLVLDAEQRV
TAAEALAHPY FESLRDTEDE PKAQKYDDSF DDVDRTLEEW KRVTYKEVLS FKPPRQLGAR
VPKETAL


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