MK10_MOUSE - dbPTM
MK10_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MK10_MOUSE
UniProt AC Q61831
Protein Name Mitogen-activated protein kinase 10
Gene Name Mapk10
Organism Mus musculus (Mouse).
Sequence Length 464
Subcellular Localization Cytoplasm . Membrane
Lipid-anchor . Nucleus . Mitochondrion . Palmitoylation regulates MAPK10 trafficking to cytoskeleton (By similarity). Recruited to the mitochondria in the presence of SARM1..
Protein Description Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock. [PubMed: 22441692]
Protein Sequence MSLHFLYYCSEPTLDVKIAFCQGFDKHVDVSSIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRSYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPVKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKSQPSPSGAAVNSSESLPPSSAVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
167PhosphorylationELDHERMSYLLYQML
CCCHHHHHHHHHHHH
20.8916483929
191UbiquitinationGIIHRDLKPSNIVVK
CEECCCCCHHHEEEE
51.17-
204UbiquitinationVKSDCTLKILDFGLA
EECCCEEEECCHHCC
24.06-
213PhosphorylationLDFGLARTAGTSFMM
CCHHCCCCCCCCCCC
24.6722499769
216PhosphorylationGLARTAGTSFMMTPY
HCCCCCCCCCCCCCH
19.1422499769
217PhosphorylationLARTAGTSFMMTPYV
CCCCCCCCCCCCCHH
15.3822499769
221PhosphorylationAGTSFMMTPYVVTRY
CCCCCCCCCHHEEEH
10.3225521595
223PhosphorylationTSFMMTPYVVTRYYR
CCCCCCCHHEEEHHC
9.8225521595
226PhosphorylationMMTPYVVTRYYRAPE
CCCCHHEEEHHCCCH
11.6922322096
311UbiquitinationYAGLTFPKLFPDSLF
CCCCCCCCCCCCCCC
59.58-
346AcetylationMLVIDPVKRISVDDA
HCCCCCCCCCCHHHH
49.77129953
396UbiquitinationEWKELIYKEVMNSEE
HHHHHHHHHHHCCHH
36.52-
462S-palmitoylationASAGPLGCCR-----
HHCCCCCCCC-----
2.02-
463S-palmitoylationSAGPLGCCR------
HCCCCCCCC------
5.70-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
221TPhosphorylationKinaseMAP2K7Q8CE90
Uniprot
223YPhosphorylationKinaseMAP2K4P47809
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
221TPhosphorylation

-
221TPhosphorylation

-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MK10_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MABP1_MOUSEMapkbp1physical
10471813

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MK10_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND TYR-223, ANDMASS SPECTROMETRY.

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