| Tag |
Content |
LipidDB ID |
LipidDB-10116-00818 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.37 |
Molecular Weight |
52530.35 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Mitogen-activated protein kinase 10 |
Protein Synonyms/Alias |
MAP kinase 10; MAPK 10; 2.7.11.24; SAPK-beta; Stress-activated protein kinase JNK3; c-Jun N-terminal kinase 3; p54-beta; |
Gene Name |
Mapk10 |
Gene Synonyms/Alias |
Jnk3; Prkm10; |
Created Date |
01-FEB-1996 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
462 | Canonical | ASAGPLGCCR***** | [1][2] | S-Palmitoylation | 463 | Canonical | SAGPLGCCR****** | [1][2] | S-Palmitoylation |
|
Organism |
Rattus norvegicus (Rat) |
NCBI Taxa ID |
10116 |
Reference |
[1] Yang G, Liu Y, Yang K, Liu R, Zhu S, Coquinco A, Wen W, Kojic L, Jia W,Cynader M. Isoform-specific palmitoylation of JNK regulates axonal development.Cell Death Differ. 2012 Apr;19(4):553-61. doi: 10.1038/cdd.2011.124. Epub 2011Sep 23.[ PMID:21941371]
[2] Yang G, Zhou X, Zhu J, Liu R, Zhang S, Coquinco A, Chen Y, Wen Y, Kojic L, JiaW, Cynader MS. JNK3 couples the neuronal stress response to inhibition ofsecretory trafficking. Sci Signal. 2013 Jul 9;6(283):ra57. doi:10.1126/scisignal.2003727.[ PMID:23838184]
|
Functional 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 beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons (By similarity). |
Sequence Annotation |
Domain: 64 359 Protein kinase. Nucleotide-binding: 70 78 ATP. Motif: 221 223 TXY. Active site: 189 189 Proton acceptor. Binding site: 93 93 ATP. Modified residue: 154 154 S-nitrosocysteine. Modified residue: 221 221 Phosphothreonine; by MAP2K7. Modified residue: 223 223 Phosphotyrosine; by MAP2K4.
|
Protein Length |
464 AA. |
Protein Sequence (Canonical) |
MSLHFLYYCS EPTLDVKIAF CQGFDKHVDV SSVVKHYNMS KSKVDNQFYS VEVGDSTFTV 60
LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH 120
KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLSAIKHL 180
HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY 240
KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN 300
RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN 360
VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA 420
VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCR 464
|
FASTA (Canonical) |
>LipidDB-10116-00818|P49187
MSLHFLYYCSEPTLDVKIAFCQGFDKHVDVSSVVKHYNMSKSKVDNQFYSVEVGDSTFTV
LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNH
KNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLSAIKHL
HSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGY
KENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVEN
RPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYIN
VWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAA
VNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
|
Gene Ontology |
|
Interpro |
|
Pfam |
|
SMART |
|
PROSITE |
|
PRINTS |
|