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Q9Z2A6 (MK15_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 15

Short name=MAP kinase 15
Short name=MAPK 15
EC=2.7.11.24
Alternative name(s):
Extracellular signal-regulated kinase 7
Short name=ERK-7
Gene names
Name:Mapk15
Synonyms:Erk7
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutively active kinase which may function as a negative regulator of cell growth. In vitro, phosphorylates FOS. Ref.1 Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation. Inhibited by dual specificity phosphatases, such as DUSP1.

Subunit structure

Interacts with TGFB1I1.

Subcellular location

Nucleus Ref.1.

Tissue specificity

Ubiquitously expressed at a weak level. Highest expression is found in testis and to a lower extent in lung. Ref.1 Ref.5

Domain

C-terminal domain, rather than the kinase activity, is required for the full function of the enzyme. This region may be a protein interaction domain that regulates kinase localization, activation and transcriptional activity. When C-terminally truncated, the enzyme shows a reduction in the Thr-Glu-Tyr (TEY) phosphorylation level, in the in vitro kinase activity, in its nuclear localization and in its inhibitory effect on cell growth. Ref.1 Ref.3

The N-terminal region (1-20) is the minimal region necessary for ubiquitination and further proteasomal degradation. Ref.1 Ref.3

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. Ref.1 Ref.3

Post-translational modification

Dually phosphorylated on Thr-176 and Tyr-178, which activates the enzyme. Autophosphorylated on threonine and tyrosine residues. Ref.1

Ubiquitinated. Ubiquitination may allow its tight kinase activity regulation and rapid turnover. May be ubiquitinated by a SCF E3 ligase. Ref.5

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 – 547547Mitogen-activated protein kinase 15
PRO_0000232639

Regions

Domain14 – 305292Protein kinase
Nucleotide binding20 – 289ATP By similarity
Region1 – 2020Ubiquitin-conjugating
Motif176 – 1783TXY

Sites

Active site1381Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue1761Phosphothreonine Ref.1
Modified residue1781Phosphotyrosine Ref.1
Modified residue4151Phosphoserine By similarity

Experimental info

Mutagenesis431K → R: Loss of autophosphorylation and activity. Ref.1
Mutagenesis1761T → A: Loss of autophosphorylation and activity. Loss of autophosphorylation and activity; when associated with F-178. Ref.1
Mutagenesis1781Y → F: Loss of autophosphorylation and activity. Loss of autophosphorylation and activity; when associated with A-176. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z2A6 [UniParc].

Last modified March 1, 2002. Version 2.
Checksum: D8B7D9955B06862F

FASTA54760,724
        10         20         30         40         50         60 
MCAAEVDRHV SQRYLIKRRL GKGAYGIVWK AMDRRTGEVV AIKKIFDAFR DQTDAQRTFR 

        70         80         90        100        110        120 
EIMLLREFGG HPNIIRLLDV IPAKNDRDIY LVFESMDTDL NAVIQKGRLL EDIHKRCIFY 

       130        140        150        160        170        180 
QLLRATKFIH SGRVIHRDQK PANVLLDAAC RVKLCDFGLA RSLSDFPEGP GGQALTEYVA 

       190        200        210        220        230        240 
TRWYRAPEVL LSSRWYTPGV DMWSLGCILG EMLRGQPLFP GTSTFHQLEL ILETIPLPSM 

       250        260        270        280        290        300 
EELQGLGSDY SALILQNLGS RPRQTLDALL PPDTPPEALD LLKRLLAFAP DKRLSAEQAL 

       310        320        330        340        350        360 
QHPYVQRFHC PDREWTRGSD VRLPVHEGDQ LSAPEYRNRL YQMILERRRN SRSPREEDLG 

       370        380        390        400        410        420 
VVASRAELRA SQRQSLKPGV LPQVLAETPA RKRGPKPQNG HGHDPEHVEV RRQSSDPLYQ 

       430        440        450        460        470        480 
LPPPGSGERP PGATGEPPSA PSGVKTHVRA VAPSLTSQAA AQAANQPLIR SDPARGGGPR 

       490        500        510        520        530        540 
AVGARRVPSR LPREAPEPRP GRRMFGISVS QGAQGAARAA LGGYSQAYGT VCRSALGRLP 


LLPGPRA 

« Hide

References

[1]"Extracellular signal-regulated kinase 7 (ERK7), a novel ERK with a C-terminal domain that regulates its activity, its cellular localization, and cell growth."
Abe M.K., Kuo W.-L., Hershenson M.B., Rosner M.R.
Mol. Cell. Biol. 19:1301-1312(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, PHOSPHORYLATION AT THR-176 AND TYR-178, MUTAGENESIS OF LYS-43; THR-176; TYR-178 AND 176-THR--TYR-178.
Strain: Sprague-Dawley.
Tissue: Testis.
[2]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 154-161, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"ERK7 is an autoactivated member of the MAPK family."
Abe M.K., Kahle K.T., Saelzler M.P., Orth K., Dixon J.E., Rosner M.R.
J. Biol. Chem. 276:21272-21279(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, CHARACTERIZATION.
[4]"ERK8, a new member of the mitogen-activated protein kinase family."
Abe M.K., Saelzler M.P., Espinosa R. III, Kahle K.T., Hershenson M.B., Le Beau M.M., Rosner M.R.
J. Biol. Chem. 277:16733-16743(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"ERK7 expression and kinase activity is regulated by the ubiquitin-proteosome pathway."
Kuo W.-L., Duke C.J., Abe M.K., Kaplan E.L., Gomes S., Rosner M.R.
J. Biol. Chem. 279:23073-23081(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF078798 mRNA. Translation: AAD12719.2.
RefSeqNP_775453.1. NM_173331.2.
XP_006241841.1. XM_006241779.1.
UniGeneRn.42898.

3D structure databases

ProteinModelPortalQ9Z2A6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z2A6. 1 interaction.
STRING10116.ENSRNOP00000012460.

Proteomic databases

PaxDbQ9Z2A6.
PRIDEQ9Z2A6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012461; ENSRNOP00000012460; ENSRNOG00000009336.
GeneID286997.
KEGGrno:286997.

Organism-specific databases

CTD225689.
RGD628675. Mapk15.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110881.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidQ9Z2A6.
KOK08293.
OMACTVKLCD.
OrthoDBEOG7VDXPC.
PhylomeDBQ9Z2A6.
TreeFamTF105101.

Gene expression databases

GenevestigatorQ9Z2A6.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio625286.
PROQ9Z2A6.

Entry information

Entry nameMK15_RAT
AccessionPrimary (citable) accession number: Q9Z2A6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 109 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