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Protein

Mitogen-activated protein kinase 15

Gene

MAPK15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner (PubMed:22948227, PubMed:24618899, PubMed:29021280, PubMed:21847093, PubMed:20733054). 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 (PubMed:22948227). Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling (PubMed:29021280). Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar-coated proteins (PubMed:24618899). Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion (PubMed:21847093). Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA (PubMed:20733054). Regulates DA transporter (DAT) activity and protein expression via activation of RhoA (PubMed:28842414). In response to H2O2 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 (PubMed:26595526). Also functions in a kinase activity-independent manner as a negative regulator of growth (By similarity). Phosphorylates in vitro FOS and MBP (PubMed:11875070, PubMed:16484222, PubMed:20638370, PubMed:19166846). During oocyte maturation, plays a key role in the microtubule organization and meiotic 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 (PubMed:21190936).By similarity12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by threonine and tyrosine phosphorylation (PubMed:11875070, PubMed:16336213, PubMed:19166846). Inhibited by dual specificity phosphatases, such as DUSP1 (By similarity). Phosphorylation and activation in response to DNA damaging agents, serum stimulation (PubMed:11875070, PubMed:16336213, PubMed:19166846). Constitutively actived when phosphorylated on Tyr-177. Activity depends on the relative rates of MAPK15 autophosphorylation and dephosphorylation by PTPN1 (PubMed:16336213).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei42ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei137Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi19 – 27ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • kinase activity Source: UniProtKB
  • MAP kinase activity Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q8TD08

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q8TD08

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mitogen-activated protein kinase 15Curated (EC:2.7.11.24)
Short name:
MAP kinase 15
Short name:
MAPK 15
Alternative name(s):
Extracellular signal-regulated kinase 7
Short name:
ERK-7
Extracellular signal-regulated kinase 8
Short name:
ERK-8
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MAPK15Imported
Synonyms:ERK7By similarity, ERK82 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000181085.14

Human Gene Nomenclature Database

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HGNCi
HGNC:24667 MAPK15

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8TD08

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Nucleus, Tight junction

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi42K → A: Not phosphorylated at Thr-175 and Tyr-177. 1 Publication1
Mutagenesisi42K → R: Loss of autophosphorylation and activity. Does not increase dopamine transporter activity. Impairs kinase activity. Does not rescue cilium assembly in MAPK15-depleted cells. 3 Publications1
Mutagenesisi59R → Q: Does not increase dopamine transporter activity. Impairs kinase activity. 1 Publication1
Mutagenesisi155D → A: Unable to induce the formation of autophagosomal structures. Is able to bind to MAP1LC3B and to colocalize with this protein to autophagosomal structures. Does not induce phosphorylation by methyl methanesulfonate. Loas of phosphorylation. Dominant negative mutant. Not phosphorylated at Thr-175 and Tyr-177. 3 Publications1
Mutagenesisi175T → A: Loss of autophosphorylation and activity. Still heavily phosphorylated at Tyr-177. Does not rescues inhibition of O-glycosylation in MAPK15-depleted cells; when associated with F-177. 3 Publications1
Mutagenesisi177Y → A: Loss of autophosphorylation and activity. Heavily phosphorylated at Thr-175. 2 Publications1
Mutagenesisi177Y → F: Does not rescues inhibition of O-glycosylation in MAPK15-depleted cells; when associated with A-175. 1 Publication1
Mutagenesisi265 – 269LDALL → ADAAA: Markedly decreases interaction with ESRRA. Impairs interaction with ESRRA; when associated with A-281 and 284-A--A-285. Loses the ability to re-localize ESRRA to the cytoplasm. Does not affect subcellular location in cytoplasm in presence of ESRRA. Loses the ability to repress ESRRA transcriptional activity. 1 Publication5
Mutagenesisi281 – 285LRRLL → ARRAA: Markedly decreases interaction with ESRRA. Impairs interaction with ESRRA; when associated with A-265 and 268-A--A-269. Loses the ability to re-localize ESRRA to the cytoplasm. Does not affect subcellular location in cytoplasm in presence of ESRRA.Loses the ability to repress ESRRA transcriptional activity. 1 Publication5
Mutagenesisi300Q → A: Impairs interaction with PCNA. Associates with chromatin. 1 Publication1
Mutagenesisi340 – 343YQMI → AQMA: Impairs interaction with GABARAP and MAP1LC3B. Affects subcellular localization in autophagosome. Does not induce autophagy. 1 Publication4
Mutagenesisi390P → A: Impairs chromatin binding; when associated with A-398. Increases kinase activity; when associated with A-398. 1 Publication1
Mutagenesisi398P → A: Impairs chromatin binding; when associated with A-390. Increases kinase activity; when associated with A-390. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
225689

Open Targets

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OpenTargetsi
ENSG00000181085

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA142671478

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5198

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2090

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MAPK15

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74760462

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002326371 – 544Mitogen-activated protein kinase 15Add BLAST544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei175Phosphothreonine3 Publications1
Modified residuei177Phosphotyrosine3 Publications1
Modified residuei449Omega-N-methylarginineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated on Thr-175 and Tyr-177; activates the enzyme.3 Publications
Ubiquitinated (PubMed:19166846). Ubiquitination may allow its tight kinase activity regulation and rapid turnover. May be ubiquitinated by a SCF E3 ligase (By similarity).By similarity1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8TD08

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8TD08

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8TD08

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q8TD08

PeptideAtlas

More...
PeptideAtlasi
Q8TD08

PRoteomics IDEntifications database

More...
PRIDEi
Q8TD08

ProteomicsDB human proteome resource

More...
ProteomicsDBi
74209
74210 [Q8TD08-2]
74211 [Q8TD08-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8TD08

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q8TD08

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed with a maximal expression in lung and kidney.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000181085 Expressed in 93 organ(s), highest expression level in right uterine tube

CleanEx database of gene expression profiles

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CleanExi
HS_MAPK15

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8TD08 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA002704

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with CSK/c-Src, ABL1, RET and TGFB1I1 (PubMed:11875070, PubMed:16484222, PubMed:16624805). Interacts with GABARAP, MAP1LC3B and GABARAPL1; controls, in a kinase-dependent fashion, both basal and starvation-induced autophagy (PubMed:22948227). Interacts with ESRRA; promotes re-localization of ESRRA to the cytoplasm through a XPO1-dependent mechanism then inhibits ESRRA transcriptional activity (PubMed:21190936). Interacts with PCNA; the interaction is chromatin binding- and kinase activity-dependent and prevents MDM2-mediated PCNA destruction by inhibiting the association of PCNA with MDM2 (PubMed:20733054). Interacts with DVL2 (By similarity). Interacts with CLIC3; MAPK15 does not phosphorylates CLIC3 (By similarity).By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
CDK2P249414EBI-1383794,EBI-375096

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
128827, 22 interactors

Protein interaction database and analysis system

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IntActi
Q8TD08, 9 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000337691

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q8TD08

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q8TD08

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8TD08

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini13 – 304Protein kinasePROSITE-ProRule annotationAdd BLAST292
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati371 – 375PXXXP motif1 Publication5
Repeati378 – 382PXXXP motif1 Publication5
Repeati386 – 390PXXXP motif; regulates binding with chromatin and interaction with PCNA1 Publication5
Repeati394 – 398PXXXP motif; regulates binding with chromatin and interaction with PCNA1 Publication5

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni265 – 285Necessary to interact with ESRRA, to regulate its subcellular localization and to inhibit its transcriptional activity1 PublicationAdd BLAST21
Regioni300 – 373Requires for interaction with GABARAP, MAP1LC3B AND GABARAPL11 PublicationAdd BLAST74

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi175 – 177TXY3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal region (1-20) is the minimal region necessary for ubiquitination and further proteasomal degradation.By similarity
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0660 Eukaryota
ENOG410XNY0 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159758

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233024

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG014652

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8TD08

KEGG Orthology (KO)

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KOi
K19603

Identification of Orthologs from Complete Genome Data

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OMAi
MCTAEVD

Database of Orthologous Groups

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OrthoDBi
741207at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8TD08

TreeFam database of animal gene trees

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TreeFami
TF105101

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01351 MAPK, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8TD08-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MCTVVDPRIV RRYLLRRQLG QGAYGIVWKA VDRRTGEVVA IKKIFDAFRD
60 70 80 90 100
KTDAQRTFRE ITLLQEFGDH PNIISLLDVI RAENDRDIYL VFEFMDTDLN
110 120 130 140 150
AVIRKGGLLQ DVHVRSIFYQ LLRATRFLHS GHVVHRDQKP SNVLLDANCT
160 170 180 190 200
VKLCDFGLAR SLGDLPEGPE DQAVTEYVAT RWYRAPEVLL SSHRYTLGVD
210 220 230 240 250
MWSLGCILGE MLRGRPLFPG TSTLHQLELI LETIPPPSEE DLLALGSGCR
260 270 280 290 300
ASVLHQLGSR PRQTLDALLP PDTSPEALDL LRRLLVFAPD KRLSATQALQ
310 320 330 340 350
HPYVQRFHCP SDEWAREADV RPRAHEGVQL SVPEYRSRVY QMILECGGSS
360 370 380 390 400
GTSREKGPEG VSPSQAHLHK PRADPQLPSR TPVQGPRPRP QSSPGHDPAE
410 420 430 440 450
HESPRAAKNV PRQNSAPLLQ TALLGNGERP PGAKEAPPLT LSLVKPSGRG
460 470 480 490 500
AAPSLTSQAA AQVANQALIR GDWNRGGGVR VASVQQVPPR LPPEARPGRR
510 520 530 540
MFSTSALQGA QGGARALLGG YSQAYGTVCH SALGHLPLLE GHHV
Length:544
Mass (Da):59,832
Last modified:June 1, 2002 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i758E0E3B9654AAC5
GO
Isoform 2 (identifier: Q8TD08-2) [UniParc]FASTAAdd to basket
Also known as: Erk8 delta

The sequence of this isoform differs from the canonical sequence as follows:
     241-254: DLLALGSGCRASVL → GAQTACRSGTGAST
     255-544: Missing.

Note: Appears not to be a CSK- and RET-dependent activated kinase.
Show »
Length:254
Mass (Da):28,696
Checksum:i88FC081FFB15644A
GO
Isoform 3 (identifier: Q8TD08-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-95: M → MGCPPSPPPPTAVRTLSA
     261-544: Missing.

Note: No experimental confirmation available.
Show »
Length:277
Mass (Da):31,112
Checksum:i07B9D39A696701D0
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1C7CYZ1A0A1C7CYZ1_HUMAN
Mitogen-activated protein kinase 15
MAPK15
276Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti113H → R in AAY44299 (PubMed:16484222).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_061535221T → K. Corresponds to variant dbSNP:rs60732298Ensembl.1
Natural variantiVAR_061536505S → P. Corresponds to variant dbSNP:rs56038219Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_01791895M → MGCPPSPPPPTAVRTLSA in isoform 3. 1 Publication1
Alternative sequenceiVSP_017919241 – 254DLLAL…RASVL → GAQTACRSGTGAST in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_017920255 – 544Missing in isoform 2. 1 PublicationAdd BLAST290
Alternative sequenceiVSP_017921261 – 544Missing in isoform 3. 1 PublicationAdd BLAST284

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY065978 mRNA Translation: AAL40897.1
AY994058 mRNA Translation: AAY44299.1
BC028034 mRNA Translation: AAH28034.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6409.2 [Q8TD08-1]

NCBI Reference Sequences

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RefSeqi
NP_620590.2, NM_139021.2 [Q8TD08-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.493169

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000338033; ENSP00000337691; ENSG00000181085 [Q8TD08-1]
ENST00000395107; ENSP00000378539; ENSG00000181085 [Q8TD08-3]
ENST00000395108; ENSP00000378540; ENSG00000181085 [Q8TD08-2]
ENST00000615253; ENSP00000483093; ENSG00000274205 [Q8TD08-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
225689

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:225689

UCSC genome browser

More...
UCSCi
uc003yzj.4 human [Q8TD08-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY065978 mRNA Translation: AAL40897.1
AY994058 mRNA Translation: AAY44299.1
BC028034 mRNA Translation: AAH28034.1
CCDSiCCDS6409.2 [Q8TD08-1]
RefSeqiNP_620590.2, NM_139021.2 [Q8TD08-1]
UniGeneiHs.493169

3D structure databases

ProteinModelPortaliQ8TD08
SMRiQ8TD08
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128827, 22 interactors
IntActiQ8TD08, 9 interactors
STRINGi9606.ENSP00000337691

Chemistry databases

BindingDBiQ8TD08
ChEMBLiCHEMBL5198
GuidetoPHARMACOLOGYi2090

PTM databases

iPTMnetiQ8TD08
PhosphoSitePlusiQ8TD08

Polymorphism and mutation databases

BioMutaiMAPK15
DMDMi74760462

Proteomic databases

EPDiQ8TD08
jPOSTiQ8TD08
MaxQBiQ8TD08
PaxDbiQ8TD08
PeptideAtlasiQ8TD08
PRIDEiQ8TD08
ProteomicsDBi74209
74210 [Q8TD08-2]
74211 [Q8TD08-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
225689
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338033; ENSP00000337691; ENSG00000181085 [Q8TD08-1]
ENST00000395107; ENSP00000378539; ENSG00000181085 [Q8TD08-3]
ENST00000395108; ENSP00000378540; ENSG00000181085 [Q8TD08-2]
ENST00000615253; ENSP00000483093; ENSG00000274205 [Q8TD08-1]
GeneIDi225689
KEGGihsa:225689
UCSCiuc003yzj.4 human [Q8TD08-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
225689
DisGeNETi225689
EuPathDBiHostDB:ENSG00000181085.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MAPK15
HGNCiHGNC:24667 MAPK15
HPAiHPA002704
neXtProtiNX_Q8TD08
OpenTargetsiENSG00000181085
PharmGKBiPA142671478

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0660 Eukaryota
ENOG410XNY0 LUCA
GeneTreeiENSGT00940000159758
HOGENOMiHOG000233024
HOVERGENiHBG014652
InParanoidiQ8TD08
KOiK19603
OMAiMCTAEVD
OrthoDBi741207at2759
PhylomeDBiQ8TD08
TreeFamiTF105101

Enzyme and pathway databases

SignaLinkiQ8TD08
SIGNORiQ8TD08

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MAPK15

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
225689

Protein Ontology

More...
PROi
PR:Q8TD08

Gene expression databases

BgeeiENSG00000181085 Expressed in 93 organ(s), highest expression level in right uterine tube
CleanExiHS_MAPK15
GenevisibleiQ8TD08 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMK15_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8TD08
Secondary accession number(s): Q2TCF9, Q8N362
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2002
Last modified: January 16, 2019
This is version 144 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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