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

 MK06_MOUSE              Reviewed;         720 AA.
Q61532; Q497T9; Q6YKB0; Q7TT30; Q80XH5; Q922U4; Q9JLU6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 3.
25-OCT-2017, entry version 146.
RecName: Full=Mitogen-activated protein kinase 6;
Short=MAP kinase 6;
Short=MAPK 6;
EC=2.7.11.24;
AltName: Full=Extracellular signal-regulated kinase 3;
Short=ERK-3;
Name=Mapk6; Synonyms=Erk3, Prkm4, Prkm6;
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 [MRNA], AND DEVELOPMENTAL STAGE.
TISSUE=Pituitary;
PubMed=10657254; DOI=10.1042/bj3460169;
Turgeon B., Saba-El-Leil M.K., Meloche S.;
"Cloning and characterization of mouse extracellular-signal-regulated
protein kinase 3 as a unique gene product of 100 kDa.";
Biochem. J. 346:169-175(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=12504858; DOI=10.1006/geno.2002.7013;
Turgeon B., Lang B.F., Meloche S.;
"The protein kinase ERK3 is encoded by a single functional gene:
genomic analysis of the ERK3 gene family.";
Genomics 80:673-680(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and Czech II;
TISSUE=Embryonic brain, Embryonic germ cell, Mammary tumor, and
Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 156-195.
STRAIN=CBA/J; TISSUE=Hematopoietic;
PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
"Novel CDC2-related protein kinases produced in murine hematopoietic
stem cells.";
Gene 124:305-306(1993).
[5]
FUNCTION IN PHOSPHORYLATION OF MAPKAPK5, SUBCELLULAR LOCATION, AND
INTERACTION WITH MAPKAPK5.
PubMed=15538386; DOI=10.1038/sj.emboj.7600467;
Schumacher S., Laass K., Kant S., Shi Y., Visel A., Gruber A.D.,
Kotlyarov A., Gaestel M.;
"Scaffolding by ERK3 regulates MK5 in development.";
EMBO J. 23:4770-4779(2004).
[6]
FUNCTION IN PHOSPHORYLATION OF MAPKAPK5, SUBCELLULAR LOCATION,
INTERACTION WITH MAPKAPK5, AND MUTAGENESIS OF ASP-171 AND SER-189.
PubMed=15577943; DOI=10.1038/sj.emboj.7600489;
Seternes O.M., Mikalsen T., Johansen B., Michaelsen E.,
Armstrong C.G., Morrice N.A., Turgeon B., Meloche S., Moens U.,
Keyse S.M.;
"Activation of MK5/PRAK by the atypical MAP kinase ERK3 defines a
novel signal transduction pathway.";
EMBO J. 23:4780-4791(2004).
[7]
INTERACTION WITH MAPK4.
PubMed=16973613; DOI=10.1074/jbc.M606693200;
Kant S., Schumacher S., Singh M.K., Kispert A., Kotlyarov A.,
Gaestel M.;
"Characterization of the atypical MAPK ERK4 and its activation of the
MAPK-activated protein kinase MK5.";
J. Biol. Chem. 281:35511-35519(2006).
[8]
INTERACTION WITH MAPKAPK5, PHOSPHORYLATION AT SER-189, AND MUTAGENESIS
OF SER-189.
PubMed=18720373; DOI=10.1002/jcp.21560;
Deleris P., Rousseau J., Coulombe P., Rodier G., Tanguay P.L.,
Meloche S.;
"Activation loop phosphorylation of the atypical MAP kinases ERK3 and
ERK4 is required for binding, activation and cytoplasmic
relocalization of MK5.";
J. Cell. Physiol. 217:778-788(2008).
[9]
INTERACTION WITH MAPKAPK5, DOMAIN FRIEDE MOTIF, AND MUTAGENESIS OF
ILE-334.
PubMed=19473979; DOI=10.1074/jbc.M109.023283;
Aberg E., Torgersen K.M., Johansen B., Keyse S.M., Perander M.,
Seternes O.M.;
"Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a
novel MAPK interaction motif.";
J. Biol. Chem. 284:19392-19401(2009).
-!- FUNCTION: Atypical MAPK protein. Phosphorylates microtubule-
associated protein 2 (MAP2) and MAPKAPK5. The precise role of the
complex formed with MAPKAPK5 is still unclear, but the complex
follows a complex set of phosphorylation events: upon interaction
with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189
and then mediates phosphorylation and activation of MAPKAPK5,
which in turn phosphorylates ERK3/MAPK6. May promote entry in the
cell cycle. {ECO:0000269|PubMed:15538386,
ECO:0000269|PubMed:15577943}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by phosphorylation at Ser-189.
-!- SUBUNIT: Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE
motif) MAPKAPK5. Interacts with UBE3A; this interaction may be
indirect and mediated by HERC2, possibly via HERC2 interaction
with NEURL4 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
cytoplasm following interaction with MAPKAPK5.
-!- DEVELOPMENTAL STAGE: Expression increases markedly from days 9 to
11 in the developing embryo, followed by a gradual decrease up to
birth. {ECO:0000269|PubMed:10657254}.
-!- DOMAIN: In contrast to classical MAPKs, the TXY motif within the
activation loop is replaced by the SEG motif, whose
phosphorylation activates the MAP kinases.
{ECO:0000269|PubMed:19473979}.
-!- PTM: Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in
catalytic activation. Phosphorylated by MAPKAPK5 at other sites.
{ECO:0000269|PubMed:18720373}.
-!- PTM: Ubiquitination at Met-1 leads to degradation by the
proteasome pathway. {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-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF132850; AAF61348.1; -; mRNA.
EMBL; AY134883; AAN64588.1; -; Genomic_DNA.
EMBL; AY134660; AAN64588.1; JOINED; Genomic_DNA.
EMBL; AY134880; AAN64588.1; JOINED; Genomic_DNA.
EMBL; AY134881; AAN64588.1; JOINED; Genomic_DNA.
EMBL; AY134882; AAN64588.1; JOINED; Genomic_DNA.
EMBL; BC006778; AAH06778.1; -; mRNA.
EMBL; BC048779; AAH48779.1; -; mRNA.
EMBL; BC052420; AAH52420.2; -; mRNA.
EMBL; BC100385; AAI00386.1; -; mRNA.
EMBL; X64607; CAA45891.1; -; mRNA.
CCDS; CCDS23342.1; -.
PIR; PN0481; PN0481.
RefSeq; NP_056621.4; NM_015806.5.
RefSeq; NP_081694.1; NM_027418.2.
RefSeq; XP_011241069.1; XM_011242767.2.
UniGene; Mm.480076; -.
ProteinModelPortal; Q61532; -.
SMR; Q61532; -.
BioGrid; 206104; 4.
STRING; 10090.ENSMUSP00000040315; -.
iPTMnet; Q61532; -.
PhosphoSitePlus; Q61532; -.
MaxQB; Q61532; -.
PaxDb; Q61532; -.
PeptideAtlas; Q61532; -.
PRIDE; Q61532; -.
Ensembl; ENSMUST00000049355; ENSMUSP00000040315; ENSMUSG00000042688.
Ensembl; ENSMUST00000168937; ENSMUSP00000129024; ENSMUSG00000042688.
GeneID; 50772; -.
KEGG; mmu:50772; -.
UCSC; uc009qsd.2; mouse.
CTD; 5597; -.
MGI; MGI:1354946; Mapk6.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00900000140906; -.
HOVERGEN; HBG104376; -.
InParanoid; Q61532; -.
KO; K06855; -.
OMA; SEHDWPI; -.
OrthoDB; EOG091G03RQ; -.
PhylomeDB; Q61532; -.
TreeFam; TF105098; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
ChiTaRS; Mapk6; mouse.
PRO; PR:Q61532; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000042688; -.
CleanEx; MM_MAPK6; -.
Genevisible; Q61532; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0032156; C:septin cytoskeleton; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0060999; P:positive regulation of dendritic spine development; IGI:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR008350; MAPK_ERK3/4.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01771; ERK3ERK4MAPK.
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;
ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 720 Mitogen-activated protein kinase 6.
/FTId=PRO_0000186258.
DOMAIN 20 316 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 26 34 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 189 191 SEG motif.
MOTIF 332 337 FRIEDE motif.
ACT_SITE 152 152 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 49 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 189 189 Phosphoserine; by PAK1, PAK2 and PAK3.
{ECO:0000305|PubMed:18720373}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000250|UniProtKB:Q16659}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:Q16659}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000250|UniProtKB:Q16659}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000250|UniProtKB:Q16659}.
CROSSLNK 1 1 Peptide (Met-Gly) (interchain with G-Cter
in ubiquitin). {ECO:0000250}.
MUTAGEN 171 171 D->A: Kinase defective mutant, abolishes
activity. {ECO:0000269|PubMed:15577943}.
MUTAGEN 189 189 S->A: Unable to activate MAPKAPK5 promote
MAPKAPK5 localization to the cytoplasm.
{ECO:0000269|PubMed:15577943,
ECO:0000269|PubMed:18720373}.
MUTAGEN 189 189 S->E: Mimicks phosphorylation state and
induces constitutive protein kinase
activity. {ECO:0000269|PubMed:15577943,
ECO:0000269|PubMed:18720373}.
MUTAGEN 334 334 I->K: Abolishes binding to MAPKAPK5.
{ECO:0000269|PubMed:19473979}.
CONFLICT 19 19 R -> T (in Ref. 2; AAN64588).
{ECO:0000305}.
CONFLICT 40 41 ND -> KY (in Ref. 2; AAN64588).
{ECO:0000305}.
CONFLICT 63 63 L -> P (in Ref. 3; AAI00386).
{ECO:0000305}.
CONFLICT 123 123 P -> S (in Ref. 1; AAF61348).
{ECO:0000305}.
CONFLICT 574 574 E -> K (in Ref. 2; AAN64588).
{ECO:0000305}.
SEQUENCE 720 AA; 82199 MW; D8BC667DEF6F62E2 CRC64;
MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK IVLTDPQSVK
HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE LNSVYIVQEY METDLANVLE
QGPLLEEHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP
HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ
MQLILDSIPV VHEEDRQELL SVIPVYIRND MTEPHRPLTQ LLPGISREAL DFLEQILTFS
PMDRLTAEEA LSHPYMSIYS FPTDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC
QFSEHDWPIH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTSYS
AEPCWQYPDH HENKYCDLEC SHTCNYKTRS SPYLDNLVWR ESEVNHYYEP KLIIDLSNWK
EQSKEKSDKR GKSKCERNGL VKAQIALEEA SQQLAERERG QGFDFDSFIA GTIQLSAQHQ
SADVVDKLND LNSSVSQLEL KSLISKSVSR EKQEKGRANL AQLGALYQSS WDSQFVSGGE
ECFLISQFCC EVRKDEHAEK ENTYTSYLDK FFSRKEDSEM LETEPVEEGK RGERGREAGL
LSGGGEFLLS KQLESIGTPQ FHSPVGSPLK SIQATLTPSA MKSSPQIPHK TYSSILKHLN


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