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Q5R7U1 (MK06_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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
Gene names
Name:MAPK6
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length721 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.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Mitogen-activated protein kinase 6
PRO_0000249009

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
Q5R7U1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: CE43B75DADD726DF

FASTA72182,678
        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 FPMDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC 

       370        380        390        400        410        420 
QFSEHDWPVH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTNYS 

       430        440        450        460        470        480 
TEPCWQYSDH HENKYCDLEC GHTCNYKTRS SSYLDNLVWR ESEVNHYYEP KLIIDLSNWK 

       490        500        510        520        530        540 
EQSKEKSDKK GKSKCERNGL VKAQIALEEA SQQLAGKERE KNQGFDFDSF IAGTIQLSSQ 

       550        560        570        580        590        600 
HEPTDVVDKL NDLNSSVSQL ELKSLISKSV SQEKQEKGMA NLAQLEALYQ SSWDSQFVNG 

       610        620        630        640        650        660 
GEDCFFINQF CEVRKDEQVE KENTYTSYLD KFFSRKEDTE MLETEPVEDG KLGERGHEEG 

       670        680        690        700        710        720 
FLNNSGEFLF NKQLESIGIP QFHSPVGSPL KSIQATLTPS AMKSSPQIPH QTYSSILKHL 


N 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860018 mRNA. Translation: CAH92169.1.
RefSeqNP_001126270.1. NM_001132798.1.

3D structure databases

ProteinModelPortalQ5R7U1.
SMRQ5R7U1. Positions 13-321.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173242.
KEGGpon:100173242.

Organism-specific databases

CTD5597.

Phylogenomic databases

HOVERGENHBG104376.
KOK06855.

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...

Entry information

Entry nameMK06_PONAB
AccessionPrimary (citable) accession number: Q5R7U1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 65 of the entry and version 1 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