Lipid Modification Database
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
GO:0005737; C:cytoplasm; ISS:UniProtKB
GO:0005739; C:mitochondrion; ISS:UniProtKB
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0005524; F:ATP binding; IDA:RGD
GO:0004705; F:JUN kinase activity; ISS:UniProtKB
GO:0007254; P:JNK cascade; ISS:UniProtKB
GO:0007258; P:JUN phosphorylation; IDA:RGD
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL
GO:0006468; P:protein phosphorylation; IDA:RGD
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR003527; MAP_kinase_CS
InterPro; IPR008351; MAPK_JNK
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF00069; Pkinase;
SMART
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS01351; MAPK;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS
PRINTS; PR01772; JNKMAPKINASE;