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Database: UniProt/SWISS-PROT
Entry: MK06_RAT
LinkDB: MK06_RAT
Original site: MK06_RAT 
ID   MK06_RAT                Reviewed;         720 AA.
AC   P27704; Q32LY4;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   16-JAN-2019, entry version 149.
DE   RecName: Full=Mitogen-activated protein kinase 6;
DE            Short=MAP kinase 6;
DE            Short=MAPK 6;
DE            EC=2.7.11.24;
DE   AltName: Full=Extracellular signal-regulated kinase 3;
DE            Short=ERK-3;
DE   AltName: Full=p55-MAPK;
GN   Name=Mapk6; Synonyms=Erk3, Prkm6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Liver;
RX   PubMed=2032290; DOI=10.1016/0092-8674(91)90098-J;
RA   Boulton T.G., Nye S.H., Robbins D.J., Ip N.Y., Radziejewska E.,
RA   Morgenbesser S.D., DePinho R.A., Panayotatos N., Cobb M.H.,
RA   Yancopoulos G.D.;
RT   "ERKs: a family of protein-serine/threonine kinases that are activated
RT   and tyrosine phosphorylated in response to insulin and NGF.";
RL   Cell 65:663-675(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Atypical MAPK protein. Phosphorylates microtubule-
CC       associated protein 2 (MAP2) and MAPKAPK5. The precise role of the
CC       complex formed with MAPKAPK5 is still unclear, but the complex
CC       follows a complex set of phosphorylation events: upon interaction
CC       with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189
CC       and then mediates phosphorylation and activation of MAPKAPK5,
CC       which in turn phosphorylates ERK3/MAPK6. May promote entry in the
CC       cell cycle (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation at Ser-189.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE
CC       motif) MAPKAPK5 (By similarity). Interacts with UBE3A; this
CC       interaction may be indirect and mediated by HERC2, possibly via
CC       HERC2 interaction with NEURL4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Translocates to the cytoplasm following
CC       interaction with MAPKAPK5. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highest levels within the nervous system,
CC       expressed in different tissues, mostly in skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed at highest levels early in
CC       development.
CC   -!- DOMAIN: In contrast to classical MAPKs, the TXY motif within the
CC       activation loop is replaced by the SEG motif, whose
CC       phosphorylation activates the MAP kinases. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in
CC       catalytic activation. Phosphorylated by MAPKAPK5 at other sites
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination at Met-1 leads to degradation by the
CC       proteasome pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA41125.1; Type=Frameshift; Positions=503; Evidence={ECO:0000305};
DR   EMBL; M64301; AAA41125.1; ALT_FRAME; mRNA.
DR   EMBL; BC109380; AAI09381.1; -; mRNA.
DR   PIR; B40033; B40033.
DR   RefSeq; NP_113810.2; NM_031622.2.
DR   RefSeq; XP_006243471.1; XM_006243409.3.
DR   UniGene; Rn.88457; -.
DR   ProteinModelPortal; P27704; -.
DR   SMR; P27704; -.
DR   STRING; 10116.ENSRNOP00000013053; -.
DR   iPTMnet; P27704; -.
DR   PhosphoSitePlus; P27704; -.
DR   jPOST; P27704; -.
DR   PaxDb; P27704; -.
DR   PRIDE; P27704; -.
DR   Ensembl; ENSRNOT00000013053; ENSRNOP00000013053; ENSRNOG00000009381.
DR   GeneID; 58840; -.
DR   KEGG; rno:58840; -.
DR   UCSC; RGD:62087; rat.
DR   CTD; 5597; -.
DR   RGD; 62087; Mapk6.
DR   eggNOG; KOG0660; Eukaryota.
DR   eggNOG; ENOG410XNY0; LUCA.
DR   GeneTree; ENSGT00940000154351; -.
DR   HOGENOM; HOG000233020; -.
DR   HOVERGEN; HBG104376; -.
DR   InParanoid; P27704; -.
DR   KO; K06855; -.
DR   OMA; RDSEVNH; -.
DR   OrthoDB; 741207at2759; -.
DR   PhylomeDB; P27704; -.
DR   TreeFam; TF105098; -.
DR   BRENDA; 2.7.11.24; 5301.
DR   Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR   PRO; PR:P27704; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000009381; Expressed in 10 organ(s), highest expression level in testis.
DR   ExpressionAtlas; P27704; baseline and differential.
DR   Genevisible; P27704; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR008350; MAPK_ERK3/4.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01771; ERK3ERK4MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN         1    720       Mitogen-activated protein kinase 6.
FT                                /FTId=PRO_0000186259.
FT   DOMAIN       20    316       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      26     34       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       189    191       SEG motif.
FT   MOTIF       332    337       FRIEDE motif.
FT   ACT_SITE    152    152       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      49     49       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     189    189       Phosphoserine; by PAK1, PAK2 and PAK3.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     386    386       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     452    452       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     554    554       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     556    556       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     683    683       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   CROSSLNK      1      1       Peptide (Met-Gly) (interchain with G-Cter
FT                                in ubiquitin). {ECO:0000250}.
SQ   SEQUENCE   720 AA;  82275 MW;  B200B215574AB84D 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
     MQLILESIPV VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS
     PMDRLTAEEA LSHPYMSIYS FPTDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC
     QFSEHDWPIH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTSYS
     AEPCWQYPDH HENKYCDLEC SHTCNYKTRS PSYLDNLVWR ESEVNHYYEP KLIIDLSNWK
     EQSKDKSDKR GKSKCERNGL VKAQIALEEA SQQLAERERG QGFDFDAFIA GTVQLSAQRE
     SADVVDKLND LNSSVSQLEM KSLISKSVSR EKQEKGRANL AQLGALYQPS WESQFVSGGE
     ECFLISQFCC EVRKDEHVEK ENTYTSYLDK FFSRKEDSEM LETEPVEEGK RGERGREAGL
     LSSGGEFLLS RQLESIGTPQ FHSPGGSPLK SIQATLTPSA MKSSPQIPHK TYSNILKHLN
//
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