MK09_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MK09_RAT
• UniProt AC: P49186
• Protein Name: Mitogen-activated protein kinase 9
• Gene Name: Mapk9
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 423
• Subcellular Localization: Cytoplasm . Nucleus . Colocalizes with POU5F1 in the nucleus.
• Protein Description: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation 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 MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation..
• Protein Sequence: MSDSKSDGQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVKDQPSDAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTGPLEGCR

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
93	Phosphorylation	ISLLNVFTPQKTLEE HHHHCCCCCCHHHHH	22.11	11823425
155	Phosphorylation	IHRDLKPSNIVVKSD ECCCCCHHHEEEECC	37.29	28689409
161	Phosphorylation	PSNIVVKSDCTLKIL HHHEEEECCCEEEEH	26.72	28689409
164	Phosphorylation	IVVKSDCTLKILDFG EEEECCCEEEEHHHH	35.76	28689409
175	Phosphorylation	LDFGLARTACTNFMM HHHHHHHHHCCHHHC	22.07	28432305
178	Phosphorylation	GLARTACTNFMMTPY HHHHHHCCHHHCCCH	29.09	28432305
183	Phosphorylation	ACTNFMMTPYVVTRY HCCHHHCCCHHHEHH	10.32	28689409
185	Phosphorylation	TNFMMTPYVVTRYYR CHHHCCCHHHEHHHC	9.82	15001544
188	Phosphorylation	MMTPYVVTRYYRAPE HCCCHHHEHHHCCCH	11.69	22108457
250	Ubiquitination	TPSAEFMKKLQPTVR CCCHHHHHHHHHHHH	56.50	-
311	Phosphorylation	IDPDKRISVDEALRH ECCCCCCCHHHHHCC	27.78	26022182
385	Phosphorylation	AAVSSKATPSQSSSI CHHCCCCCCCCCCCH	27.49	28689409
387	Phosphorylation	VSSKATPSQSSSIND HCCCCCCCCCCCHHH	38.04	28689409
389	Phosphorylation	SKATPSQSSSINDIS CCCCCCCCCCHHHHH	30.32	28689409
390	Phosphorylation	KATPSQSSSINDISS CCCCCCCCCHHHHHC	27.83	25575281
391	Phosphorylation	ATPSQSSSINDISSM CCCCCCCCHHHHHCC	30.56	25575281
396	Phosphorylation	SSSINDISSMSTEHT CCCHHHHHCCCCCCC	23.89	28689409
397	Phosphorylation	SSINDISSMSTEHTL CCHHHHHCCCCCCCC	19.65	28689409
399	Phosphorylation	INDISSMSTEHTLAS HHHHHCCCCCCCCCC	32.37	28689409
400	Phosphorylation	NDISSMSTEHTLASD HHHHCCCCCCCCCCC	24.12	28689409
403	Phosphorylation	SSMSTEHTLASDTDS HCCCCCCCCCCCCCC	20.14	25575281
406	Phosphorylation	STEHTLASDTDSSLD CCCCCCCCCCCCCCC	44.12	28689409
408	Phosphorylation	EHTLASDTDSSLDAS CCCCCCCCCCCCCCC	34.97	28689409
410	Phosphorylation	TLASDTDSSLDASTG CCCCCCCCCCCCCCC	34.59	25575281
411	Phosphorylation	LASDTDSSLDASTGP CCCCCCCCCCCCCCC	32.83	28689409
415	Phosphorylation	TDSSLDASTGPLEGC CCCCCCCCCCCCCCC	33.30	25575281
416	Phosphorylation	DSSLDASTGPLEGCR CCCCCCCCCCCCCCC	44.53	25575281

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
183	T	Phosphorylation	Kinase	MAP2K7	Q4KSH7	Uniprot
185	Y	Phosphorylation	Kinase	MAP2K4	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
183	T	Phosphorylation	Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MK09_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of MK09_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.