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P27704 (MK06_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 6

Short name=MAP kinase 6
Short name=MAPK 6
EC=2.7.11.24
Alternative name(s):
Extracellular signal-regulated kinase 3
Short name=ERK-3
p55-MAPK
Gene names
Name:Mapk6
Synonyms:Erk3, Prkm6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by phosphorylation at Ser-189 By similarity.

Subunit structure

Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE motif) MAPKAPK5 By similarity. Interacts with UBE3A; this interaction may be indirect and mediated by HERC2, possibly via HERC2 interaction with NEURL4 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Translocates to the cytoplasm following interaction with MAPKAPK5 By similarity.

Tissue specificity

Highest levels within the nervous system, expressed in different tissues, mostly in skeletal muscle.

Developmental stage

Expressed at highest levels early in development.

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 By similarity.

Post-translational modification

Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in catalytic activation. Phosphorylated by MAPKAPK5 at other sites By similarity.

Ubiquitination at Met-1 leads to degradation by the proteasome pathway By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAA41125.1 differs from that shown. Reason: Frameshift at position 503.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Mitogen-activated protein kinase 6
PRO_0000186259

Regions

Domain20 – 316297Protein kinase
Nucleotide binding26 – 349ATP By similarity
Motif189 – 1913SEG motif
Motif332 – 3376FRIEDE motif

Sites

Active site1521Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1891Phosphoserine; by PAK1, PAK2 and PAK3 By similarity
Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P27704 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B200B215574AB84D

FASTA72082,275
        10         20         30         40         50         60 
MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK IVLTDPQSVK 

        70         80         90        100        110        120 
HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE LNSVYIVQEY METDLANVLE 

       130        140        150        160        170        180 
QGPLLEEHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP 

       190        200        210        220        230        240 
HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ 

       250        260        270        280        290        300 
MQLILESIPV VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS 

       310        320        330        340        350        360 
PMDRLTAEEA LSHPYMSIYS FPTDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC 

       370        380        390        400        410        420 
QFSEHDWPIH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTSYS 

       430        440        450        460        470        480 
AEPCWQYPDH HENKYCDLEC SHTCNYKTRS PSYLDNLVWR ESEVNHYYEP KLIIDLSNWK 

       490        500        510        520        530        540 
EQSKDKSDKR GKSKCERNGL VKAQIALEEA SQQLAERERG QGFDFDAFIA GTVQLSAQRE 

       550        560        570        580        590        600 
SADVVDKLND LNSSVSQLEM KSLISKSVSR EKQEKGRANL AQLGALYQPS WESQFVSGGE 

       610        620        630        640        650        660 
ECFLISQFCC EVRKDEHVEK ENTYTSYLDK FFSRKEDSEM LETEPVEEGK RGERGREAGL 

       670        680        690        700        710        720 
LSSGGEFLLS RQLESIGTPQ FHSPGGSPLK SIQATLTPSA MKSSPQIPHK TYSNILKHLN 

« Hide

References

« Hide 'large scale' references
[1]"ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF."
Boulton T.G., Nye S.H., Robbins D.J., Ip N.Y., Radziejewska E., Morgenbesser S.D., DePinho R.A., Panayotatos N., Cobb M.H., Yancopoulos G.D.
Cell 65:663-675(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain and Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64301 mRNA. Translation: AAA41125.1. Frameshift.
BC109380 mRNA. Translation: AAI09381.1.
PIRB40033.
RefSeqNP_113810.2. NM_031622.2.
XP_006243471.1. XM_006243409.1.
UniGeneRn.88457.

3D structure databases

ProteinModelPortalP27704.
SMRP27704. Positions 13-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000013053.

PTM databases

PhosphoSiteP27704.

Proteomic databases

PaxDbP27704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000013053; ENSRNOP00000013053; ENSRNOG00000009381.
GeneID58840.
KEGGrno:58840.
UCSCRGD:62087. rat.

Organism-specific databases

CTD5597.
RGD62087. Mapk6.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOGENOMHOG000233020.
HOVERGENHBG104376.
InParanoidP27704.
KOK06855.
OMAEHDWPIH.
OrthoDBEOG780RKS.
PhylomeDBP27704.
TreeFamTF105098.

Enzyme and pathway databases

BRENDA2.7.11.24. 5301.

Gene expression databases

GenevestigatorP27704.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR008350. MAPK_ERK3/4.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01771. ERK3ERK4MAPK.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio611410.
PROP27704.

Entry information

Entry nameMK06_RAT
AccessionPrimary (citable) accession number: P27704
Secondary accession number(s): Q32LY4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families