MAP3K9
entrez
4293
canonical
uniprot
P80192
canonical
ensembl
ENSG00000006432
resolver
ensp
ENSP00000370649
resolver
ensp
ENSP00000451038
resolver
ensp
ENSP00000451263
resolver
ensp
ENSP00000451612
resolver
ensp
ENSP00000451921
resolver
enst
ENST00000381250
resolver
enst
ENST00000553414
resolver
genesymbol
MAP3K9
resolver
genesymbol_syn
MLK1
resolver
genesymbol_syn
PRKE1
resolver
hgnc
HGNC:6861
resolver
uniprot
A3KN85
resolver
uniprot
B4DZC4
resolver
uniprot
G3V347
resolver
uniprot
J3KPI6
resolver
uniprot
Q0D2G7
resolver
uniprot
Q6EH31
resolver
uniprot
Q8NEB1
resolver
uniprot
Q9H2N5
resolver
uniprot_entry
B4DZC4_HUMAN
resolver
uniprot_entry
G3V347_HUMAN
resolver
uniprot_entry
J3KPI6_HUMAN
resolver
uniprot_entry
M3K9_HUMAN
resolver
uniprot_entry
Q8NEB1_HUMAN
resolver
uniprot_sec
A3KN85
resolver
uniprot_sec
Q0D2G7
resolver
uniprot_sec
Q6EH31
resolver
uniprot_sec
Q9H2N5
resolver
activity_regulation
ACTIVITY REGULATION: Homodimerization via the leucine zipper domains is required for autophosphorylation of multiple sites in the activation loop and subsequent activation. Autophosphorylation at Thr-312 is the key step in activation of MAP3K9/MLK1 and is required for full phosphorylation. Autophosphorylation at Thr-304 and Ser-308 have been shown to be of secondary importance in the activation of MAP3K9/MLK1. CEP-1347 and many indolocarbazole analogs have been shown to act as inhibitors of MAP3K9/MLK1 activity. {ECO:0000269|PubMed:11325962, ECO:0000269|PubMed:11755341, ECO:0000269|PubMed:15610029}.
uniprot
proteins
amino_acid_sequence
MEPSRALLGCLASAAAAAPPGEDGAGAGAEEEEEEEEEAAAAVGPGELGCDAPLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGGEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEMPKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSDFQHKFTVQASPTMDKRKSLINSRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELASGDEGSPQRREKANGLSTPSESPHFHLGLKSLVDGYKQWSSSAPNLVKGPRSSPALPGFTSLMEMEDEDSEGPGSGESRLQHSPSQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRGGAHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPLEEPEPPAREEKKRREGLFQRSSRPRRSTSPPSRKLFKKEEPMLLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLSPCTHNPLVNVRVERFKRDPNQSLTPTHVTLTTPSQPSSHRRTPSDGALKPETLLASRSPSSNGLSPSPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQQDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSTSPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPFQAGPLPPTERTLLDLDAEGQSQDSTVPLCRAELNTHRPAPYEIQQEFWS
uniprot
proteins
disease_involvement
DISEASE: Note=May play a role in esophageal cancer susceptibility and/or development.
uniprot
proteins
ec_number
2.7.11.25
uniprot
proteins
function
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Also plays a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. {ECO:0000269|PubMed:11416147, ECO:0000269|PubMed:15610029}.
uniprot
proteins
mass_dalton
121895
uniprot
proteins
mutagenesis
MUTAGEN 171; /note="K->A: Loss of kinase activity and threonine phosphorylation."; /evidence="ECO:0000269|PubMed:15610029"; MUTAGEN 304; /note="T->A: Reduces threonine phosphorylation. Impairs JNK activation."; /evidence="ECO:0000269|PubMed:15610029"; MUTAGEN 305; /note="T->A: Little effect on threonine phosphorylation. Mildly impairs JNK activation."; /evidence="ECO:0000269|PubMed:15610029"; MUTAGEN 308; /note="S->A: Impairs JNK activation."; /evidence="ECO:0000269|PubMed:15610029"; MUTAGEN 312; /note="T->A: Loss of threonine phosphorylation. Strongly impairs JNK activation."; /evidence="ECO:0000269|PubMed:15610029
uniprot
proteins
post_translational_modification
PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-312 is likely to be the main autophosphorylation site. Autophosphorylation also occurs on Thr-304 and Ser-308. {ECO:0000269|PubMed:11325962, ECO:0000269|PubMed:15610029}.
uniprot
proteins
protein_family
MAP kinase kinase kinase subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
STE Ser/Thr protein kinase family
uniprot
proteins
pubmed
11325962
uniprot
proteins
pubmed
11416147
uniprot
proteins
pubmed
11755341
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15610029
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18241037
uniprot
proteins
pubmed
18714982
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8477742
uniprot
proteins
sequence_length
1104
uniprot
proteins