Q9SFB6 · M3KE2_ARATH
- ProteinMAP3K epsilon protein kinase 2
- GeneMAP3KE2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1367 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells (PubMed:15292395).
Required for the normal functioning of the plasma membrane in developing pollen (PubMed:16965555).
Involved in the regulation of cell expansion and embryo development (PubMed:23087695).
Required for the normal functioning of the plasma membrane in developing pollen (PubMed:16965555).
Involved in the regulation of cell expansion and embryo development (PubMed:23087695).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | microtubule organizing center | |
Cellular Component | nucleolus | |
Cellular Component | plasma membrane | |
Cellular Component | vacuole | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cell division | |
Biological Process | protein autophosphorylation | |
Biological Process | regulation of cell division |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMAP3K epsilon protein kinase 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SFB6
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Accumulates in the nucleolus during interphase (PubMed:15292395).
Localized to the plasma membrane in developing pollen grains (By similarity).
Localized to the plasma membrane in developing pollen grains (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Pollen lethality in plants lacking both MAP3KE1 and MAP3KE2, associated with plasma membrane irregularities following pollen mitosis I (PubMed:16965555).
Smaller plants with shorter roots due to reduced cell elongation in roots and reduced cell expansion in rosette leaves, as well as embryos arrest in the early stages of development (PubMed:23087695).
Smaller plants with shorter roots due to reduced cell elongation in roots and reduced cell expansion in rosette leaves, as well as embryos arrest in the early stages of development (PubMed:23087695).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 80 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000432225 | 1-1367 | MAP3K epsilon protein kinase 2 | |||
Sequence: MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIGQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADFNTHSVVGTPYWMAPEVIELSGVCAASDIWSVGCTIIELLTCVPPYYDLQPMPALYRIVQDDTPPIPDSLSPDITDFLRLCFKKDSRQRPDAKTLLSHPWIRNSRRALRSSLRHSGTIRYMKETDSSSEKDAEGSQEVVESVSAEKVEVTKTNSKSKLPVIGGASFRSEKDQSSPSDLGEEGTDSEDDINSDQGPTLSMHDKSSRQSGTCSISSDAKGTSQDVLENHEKYDRDEIPGNLETEASEGRRNTLATKLVGKEYSIQSSHSFSQKGEDGLRKAVKTPSSFGGNELTRFSDPPGDASLHDLFHPLDKVPEGKTNEASTSTPTANVNQGDSPVADGGKNDLATKLRARIAQKQMEGETGHSQDGGDLFRLMMGVLKDDVLNIDDLVFDEKVPPENLFPLQAVEFSRLVSSLRPDESEDAIVTSSLKLVAMFRQRPGQKAVFVTQNGFLPLMDLLDIPKSRVICAVLQLINEIVKDNTDFLENACLVGLIPLVMSFAGFERDRSREIRKEAAYFLQQLCQSSPLTLQMFISCRGIPVLVGFLEADYAKHREMVHLAIDGMWQVFKLKKSTSRNDFCRIAAKNGILLRLVNTLYSLSEATRLASISGDALILDGQTPRARSGQLDPNNPIFSQRETSPSVIDHPDGLKTRNGGGEEPSHALTSNSQSSDVHQPDALHPDGDRPRLSSVVADATEDVIQQHRISLSANRTSTDKLQKLAEGASNGFPVTQPDQVRPLLSLLEKEPPSRKISGQLDYVKHIAGIERHESRLPLLYASDEKKTNGDLEFIMAEFAEVSGRGKENGNLDTAPRYSSKTMTKKVMAIERVASTCGIASQTASGVLSGSGVLNARPGSTTSSGLLAHALSADVSMDYLEKVADLLLEFARAETTVKSYMCSQSLLSRLFQMFNRVEPPILLKILECTNHLSTDPNCLENLQRADAIKQLIPNLELKEGPLVYQIHHEVLSALFNLCKINKRRQEQAAENGIIPHLMLFVMSDSPLKQYALPLLCDMAHASRNSREQLRAHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDVDQKVEQAFLKKDAIQKLVNFFQNCPERHFVHILEPFLKIITKSSSINKTLALNGLTPLLIARLDHQDAIARLNLLKLIKAVYEKHPKPKQLIVENDLPQKLQNLIEERRDGQRSGGQVLVKQMATSLLKALHINTIL |
Post-translational modification
Autophosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in both the sporophytic and the gametophytic tissues, especially in dividing cells. Mostly present in flower buds and mature flowers. Accumulates also in embryos and in roots.
Induction
Expression is cell cycle-regulated, with higher expression in G2-M phases.
Developmental stage
Expressed during embryo development.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-274 | Protein kinase | ||||
Sequence: YMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIGQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADFNTHSVVGTPYWMAPEVIELSGVCAASDIWSVGCTIIELLTCVPPYYDLQPMPALYRIVQDDTPPIPDSLSPDITDFLRLCFKKDSRQRPDAKTLLSHPWI | ||||||
Repeat | 25-62 | HEAT 1 | ||||
Sequence: EIGKGAYGRVYIGLDLENGDFVAIKQVSLENIGQEDLN | ||||||
Repeat | 86-125 | HEAT 2 | ||||
Sequence: LKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYI | ||||||
Repeat | 218-256 | HEAT 3 | ||||
Sequence: PYYDLQPMPALYRIVQDDTPPIPDSLSPDITDFLRLCFK | ||||||
Region | 285-422 | Disordered | ||||
Sequence: LRHSGTIRYMKETDSSSEKDAEGSQEVVESVSAEKVEVTKTNSKSKLPVIGGASFRSEKDQSSPSDLGEEGTDSEDDINSDQGPTLSMHDKSSRQSGTCSISSDAKGTSQDVLENHEKYDRDEIPGNLETEASEGRRN | ||||||
Compositional bias | 289-309 | Basic and acidic residues | ||||
Sequence: GTIRYMKETDSSSEKDAEGSQ | ||||||
Compositional bias | 362-393 | Polar residues | ||||
Sequence: INSDQGPTLSMHDKSSRQSGTCSISSDAKGTS | ||||||
Compositional bias | 394-414 | Basic and acidic residues | ||||
Sequence: QDVLENHEKYDRDEIPGNLET | ||||||
Region | 437-513 | Disordered | ||||
Sequence: SSHSFSQKGEDGLRKAVKTPSSFGGNELTRFSDPPGDASLHDLFHPLDKVPEGKTNEASTSTPTANVNQGDSPVADG | ||||||
Compositional bias | 490-509 | Polar residues | ||||
Sequence: KTNEASTSTPTANVNQGDSP | ||||||
Repeat | 538-576 | HEAT 4 | ||||
Sequence: SQDGGDLFRLMMGVLKDDVLNIDDLVFDEKVPPENLFPL | ||||||
Repeat | 577-614 | HEAT 5 | ||||
Sequence: QAVEFSRLVSSLRPDESEDAIVTSSLKLVAMFRQRPGQ | ||||||
Repeat | 633-658 | HEAT 6 | ||||
Sequence: IPKSRVICAVLQLINEIVKDNTDFLE | ||||||
Repeat | 659-700 | HEAT 7 | ||||
Sequence: NACLVGLIPLVMSFAGFERDRSREIRKEAAYFLQQLCQSSPL | ||||||
Repeat | 704-742 | HEAT 8 | ||||
Sequence: MFISCRGIPVLVGFLEADYAKHREMVHLAIDGMWQVFKL | ||||||
Region | 792-860 | Disordered | ||||
Sequence: PRARSGQLDPNNPIFSQRETSPSVIDHPDGLKTRNGGGEEPSHALTSNSQSSDVHQPDALHPDGDRPRL | ||||||
Compositional bias | 795-814 | Polar residues | ||||
Sequence: RSGQLDPNNPIFSQRETSPS | ||||||
Compositional bias | 831-847 | Polar residues | ||||
Sequence: EPSHALTSNSQSSDVHQ | ||||||
Repeat | 850-888 | HEAT 9 | ||||
Sequence: ALHPDGDRPRLSSVVADATEDVIQQHRISLSANRTSTDK | ||||||
Repeat | 906-943 | HEAT 10 | ||||
Sequence: DQVRPLLSLLEKEPPSRKISGQLDYVKHIAGIERHESR | ||||||
Repeat | 1045-1066 | HEAT 11 | ||||
Sequence: DYLEKVADLLLEFARAETTVKS | ||||||
Repeat | 1067-1105 | HEAT 12 | ||||
Sequence: YMCSQSLLSRLFQMFNRVEPPILLKILECTNHLSTDPNC | ||||||
Repeat | 1112-1150 | HEAT 13 | ||||
Sequence: ADAIKQLIPNLELKEGPLVYQIHHEVLSALFNLCKINKR | ||||||
Repeat | 1154-1191 | HEAT 14 | ||||
Sequence: QAAENGIIPHLMLFVMSDSPLKQYALPLLCDMAHASRN | ||||||
Repeat | 1196-1236 | HEAT 15 | ||||
Sequence: LRAHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDVDQKVEQ | ||||||
Repeat | 1257-1280 | HEAT 16 | ||||
Sequence: RHFVHILEPFLKIITKSSSINKTL | ||||||
Repeat | 1281-1317 | HEAT 17 | ||||
Sequence: ALNGLTPLLIARLDHQDAIARLNLLKLIKAVYEKHPK | ||||||
Repeat | 1347-1367 | HEAT 18 | ||||
Sequence: QVLVKQMATSLLKALHINTIL |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,367
- Mass (Da)151,137
- Last updated2000-05-01 v1
- Checksum7618AFA6B41A227C
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1I9LPC2 | A0A1I9LPC2_ARATH | MAPKKK6 | 1343 | ||
A0A1I9LPC3 | A0A1I9LPC3_ARATH | MAPKKK6 | 1182 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 289-309 | Basic and acidic residues | ||||
Sequence: GTIRYMKETDSSSEKDAEGSQ | ||||||
Compositional bias | 362-393 | Polar residues | ||||
Sequence: INSDQGPTLSMHDKSSRQSGTCSISSDAKGTS | ||||||
Compositional bias | 394-414 | Basic and acidic residues | ||||
Sequence: QDVLENHEKYDRDEIPGNLET | ||||||
Compositional bias | 490-509 | Polar residues | ||||
Sequence: KTNEASTSTPTANVNQGDSP | ||||||
Compositional bias | 795-814 | Polar residues | ||||
Sequence: RSGQLDPNNPIFSQRETSPS | ||||||
Compositional bias | 831-847 | Polar residues | ||||
Sequence: EPSHALTSNSQSSDVHQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC013483 EMBL· GenBank· DDBJ | AAF21208.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74627.1 EMBL· GenBank· DDBJ | Genomic DNA |