Mapk15
entrez
286997
canonical
uniprot
Q9Z2A6
canonical
ensembl
ENSRNOG00000009336
resolver
ensembl
ENSRNOG00060021050
resolver
ensembl
ENSRNOG00065009415
resolver
ensp
ENSRNOP00000012460
resolver
ensp
ENSRNOP00060030033
resolver
ensp
ENSRNOP00065011266
resolver
enst
ENSRNOT00000012461
resolver
enst
ENSRNOT00060036494
resolver
enst
ENSRNOT00065015061
resolver
genesymbol
Mapk15
resolver
genesymbol_syn
Erk7
resolver
genesymbol_syn
Erk8
resolver
uniprot_entry
MK15_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated by threonine and tyrosine phosphorylation. Inhibited by dual specificity phosphatases, such as DUSP1 (By similarity). Phosphorylation and activation in response to DNA damaging agents, serum stimulation. Constitutively activated when phosphorylated on Tyr-178. Activity depends on the relative rates of MAPK15 autophosphorylation and dephosphorylation by PTPN1 (By similarity). {ECO:0000250|UniProtKB:Q8TD08, ECO:0000269|PubMed:9891064}.
uniprot
proteins
amino_acid_sequence
MCAAEVDRHVSQRYLIKRRLGKGAYGIVWKAMDRRTGEVVAIKKIFDAFRDQTDAQRTFREIMLLREFGGHPNIIRLLDVIPAKNDRDIYLVFESMDTDLNAVIQKGRLLEDIHKRCIFYQLLRATKFIHSGRVIHRDQKPANVLLDAACRVKLCDFGLARSLSDFPEGPGGQALTEYVATRWYRAPEVLLSSRWYTPGVDMWSLGCILGEMLRGQPLFPGTSTFHQLELILETIPLPSMEELQGLGSDYSALILQNLGSRPRQTLDALLPPDTPPEALDLLKRLLAFAPDKRLSAEQALQHPYVQRFHCPDREWTRGSDVRLPVHEGDQLSAPEYRNRLYQMILERRRNSRSPREEDLGVVASRAELRASQRQSLKPGVLPQVLAETPARKRGPKPQNGHGHDPEHVEVRRQSSDPLYQLPPPGSGERPPGATGEPPSAPSGVKTHVRAVAPSLTSQAAAQAANQPLIRSDPARGGGPRAVGARRVPSRLPREAPEPRPGRRMFGISVSQGAQGAARAALGGYSQAYGTVCRSALGRLPLLPGPRA
uniprot
proteins
ec_number
2.7.11.24
uniprot
proteins
function
FUNCTION: Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner. Controls both, basal and starvation-induced autophagy throught its interaction with GABARAP, MAP1LC3B and GABARAPL1 leading to autophagosome formation, SQSTM1 degradation and reduced MAP1LC3B inhibitory phosphorylation. Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling. Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar-coated proteins. Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion. Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA. Regulates DA transporter (DAT) activity and protein expression via activation of RhoA. In response to H(2)O(2) treatment phosphorylates ELAVL1, thus preventing it from binding to the PDCD4 3'UTR and rendering the PDCD4 mRNA accessible to miR-21 and leading to its degradation and loss of protein expression (By similarity). Also functions in a kinase activity-independent manner as a negative regulator of growth (PubMed:9891064). Phosphorylates in vitro FOS and MBP (PubMed:11875070). During oocyte maturation, plays a key role in the microtubule organization and mei- otic cell cycle progression in oocytes, fertilized eggs, and early embryos (By similarity). Interacts with ESRRA promoting its re-localization from the nucleus to the cytoplasm and then prevents its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q80Y86, ECO:0000250|UniProtKB:Q8TD08, ECO:0000269|PubMed:11875070, ECO:0000269|PubMed:9891064}.
uniprot
proteins
mass_dalton
60724
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="K->R: Loss of autophosphorylation and activity."; /evidence="ECO:0000269|PubMed:9891064"; MUTAGEN 176; /note="T->A: Loss of autophosphorylation and activity. Loss of autophosphorylation and activity; when associated with F-178."; /evidence="ECO:0000269|PubMed:9891064"; MUTAGEN 178; /note="Y->F: Loss of autophosphorylation and activity. Loss of autophosphorylation and activity; when associated with A-176."; /evidence="ECO:0000269|PubMed:9891064
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated on Thr-176 and Tyr-178; activates the enzyme. {ECO:0000269|PubMed:9891064}.; PTM: Dephosphorylated by PTPN1. {ECO:0000250|UniProtKB:Q8TD08}.; PTM: Ubiquitinated. Ubiquitination may allow its tight kinase activity regulation and rapid turnover. May be ubiquitinated by a SCF E3 ligase. {ECO:0000269|PubMed:15033983}.
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
MAP kinase subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11287416
uniprot
proteins
pubmed
11875070
uniprot
proteins
pubmed
15033983
uniprot
proteins
pubmed
9880541
uniprot
proteins
pubmed
9891064
uniprot
proteins
sequence_length
547
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8TD08}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8TD08}. Golgi apparatus {ECO:0000250|UniProtKB:Q8TD08}. Nucleus {ECO:0000269|PubMed:9880541, ECO:0000269|PubMed:9891064}. Cytoplasm {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q80Y86}. Note=Co-localizes to the cytoplasm only in presence of ESRRA. Translocates to the nucleus upon activation (By similarity). At prometaphase I, metaphase I (MI), anaphase I, telophase I, and metaphase II (MII) stages, is stably detected at the spindle (By similarity). {ECO:0000250|UniProtKB:Q80Y86, ECO:0000250|UniProtKB:Q8TD08}.
uniprot
proteins