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UniProtKB - P28482 (MK01_HUMAN)

Entry version 222 (13 Feb 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Mitogen-activated protein kinase 1

Gene

MAPK1

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

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity).4 PublicationsBy similarity25 Publications
Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.1 Publication

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<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

Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-185 and Tyr-187 in response to external stimuli like insulin or NGF. Both phosphorylations are required for activity. This phosphorylation causes dramatic conformational changes, which enable full activation and interaction of MAPK1/ERK2 with its substrates. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP1, DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors.2 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 sitei54ATPPROSITE-ProRule annotation1
Binding sitei54Inhibitor6 Publications1
Binding sitei108Inhibitor; via amide nitrogen and carbonyl oxygen6 Publications1
Binding sitei114Inhibitor6 Publications1
<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 sitei149Proton acceptorPROSITE-ProRule annotation1
Binding sitei154Inhibitor6 Publications1
Binding sitei166Inhibitor6 Publications1
Binding sitei167Inhibitor6 Publications1

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 bindingi31 – 39ATPPROSITE-ProRule annotation9
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi259 – 277Add BLAST19

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionDNA-binding, Kinase, Repressor, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle, Host-virus interaction, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.24 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-111995 phospho-PLA2 pathway
R-HSA-112409 RAF-independent MAPK1/3 activation
R-HSA-112411 MAPK1 (ERK2) activation
R-HSA-1295596 Spry regulation of FGF signaling
R-HSA-162658 Golgi Cisternae Pericentriolar Stack Reorganization
R-HSA-170968 Frs2-mediated activation
R-HSA-198753 ERK/MAPK targets
R-HSA-202670 ERKs are inactivated
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-437239 Recycling pathway of L1
R-HSA-444257 RSK activation
R-HSA-445144 Signal transduction by L1
R-HSA-450341 Activation of the AP-1 family of transcription factors
R-HSA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5654727 Negative regulation of FGFR2 signaling
R-HSA-5654732 Negative regulation of FGFR3 signaling
R-HSA-5654733 Negative regulation of FGFR4 signaling
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5668599 RHO GTPases Activate NADPH Oxidases
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5674499 Negative feedback regulation of MAPK pathway
R-HSA-5675221 Negative regulation of MAPK pathway
R-HSA-6798695 Neutrophil degranulation
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-74749 Signal attenuation
R-HSA-879415 Advanced glycosylation endproduct receptor signaling
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK
R-HSA-8939211 ESR-mediated signaling
R-HSA-8940973 RUNX2 regulates osteoblast differentiation
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-9627069 Regulation of the apoptosome activity
R-HSA-982772 Growth hormone receptor signaling

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

More...SignaLinki		P28482

SIGNOR Signaling Network Open Resource

More...SIGNORi		P28482

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P28482 Predicted

MoonProt database of moonlighting proteins

More...MoonProti		P28482

<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 1 (EC:2.7.11.24)
Short name:
MAP kinase 1
Short name:
MAPK 1
Alternative name(s):
ERT1
Extracellular signal-regulated kinase 2
Short name:
ERK-2
MAP kinase isoform p42
Short name:
p42-MAPK
Mitogen-activated protein kinase 2
Short name:
MAP kinase 2
Short name:
MAPK 2
<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:MAPK1
Synonyms:ERK2, PRKM1, PRKM2
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 22

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000100030.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:6871 MAPK1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		176948 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P28482

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

<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>Mutagenesisi54K → R: Does not inhibit interaction with MAP2K1. 1 Publication1
Mutagenesisi176 – 179Missing : Inhibits homodimerization and interaction with TPR. 1 Publication4
Mutagenesisi185T → A: Inhibits interaction with TPR; when associated with A-187. 1 Publication1
Mutagenesisi187Y → A: Inhibits interaction with TPR; when associated with A-185. 1 Publication1
Mutagenesisi234L → A: Inhibits interaction with TPR. 1 Publication1
Mutagenesisi318D → A: Loss of dephosphorylation by PTPRJ. 2 Publications1
Mutagenesisi318D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-321. 2 Publications1
Mutagenesisi321D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-318. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5594

MalaCards human disease database

More...MalaCardsi		MAPK1

Open Targets

More...OpenTargetsi		ENSG00000100030

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		261330 Distal 22q11.2 microdeletion syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30616

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4040

Drug and drug target database

More...DrugBanki		DB07264 (S)-N-(1-(3-CHLORO-4-FLUOROPHENYL)-2-HYDROXYETHYL)-4-(4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL)-1H-PYRROLE-2-CARBOXAMIDE
DB08521 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE
DB08513 [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID
DB01169 Arsenic trioxide
DB01064 Isoprenaline
DB07010 N-BENZYL-4-[4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL]-1H-PYRROLE-2-CARBOXAMIDE
DB02116 Olomoucine
DB02482 Phosphonothreonine
DB02733 Purvalanol
DB04338 SB220025
DB11120 Turpentine

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1495

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MAPK1

Domain mapping of disease mutations (DMDM)

More...DMDMi		119554

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00001862472 – 360Mitogen-activated protein kinase 1Add BLAST359

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 residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei29Phosphoserine; by SGK11 Publication1
Modified residuei185Phosphothreonine; by MAP2K1 and MAP2K2Combined sources1
Modified residuei187Phosphotyrosine; by MAP2K1 and MAP2K2Combined sources2 Publications1
Modified residuei190Phosphothreonine; by autocatalysis1 Publication1
Modified residuei246Phosphoserine1 Publication1
Modified residuei248Phosphoserine1 Publication1
Modified residuei284PhosphoserineCombined 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

Phosphorylated upon KIT and FLT3 signaling (By similarity). Dually phosphorylated on Thr-185 and Tyr-187, which activates the enzyme. Undergoes regulatory phosphorylation on additional residues such as Ser-246 and Ser-248 in the kinase insert domain (KID) These phosphorylations, which are probably mediated by more than one kinase, are important for binding of MAPK1/ERK2 to importin-7 (IPO7) and its nuclear translocation. In addition, autophosphorylation of Thr-190 was shown to affect the subcellular localization of MAPK1/ERK2 as well. Ligand-activated ALK induces tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-187. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. DUSP3 and DUSP6 dephosphorylate specifically MAPK1/ERK2 and MAPK3/ERK1 whereas DUSP9 dephosphorylates a broader range of MAPKs. Dephosphorylated by DUSP1 at Thr-185 and Tyr-187.By similarity7 Publications
ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P28482

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P28482

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

More...PaxDbi		P28482

PeptideAtlas

More...PeptideAtlasi		P28482

PRoteomics IDEntifications database

More...PRIDEi		P28482

ProteomicsDB human proteome resource

More...ProteomicsDBi		54488

2D gel databases

USC-OGP 2-DE database

More...OGPi		P28482

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P28482

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

More...PhosphoSitePlusi		P28482

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P28482

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000100030 Expressed in 241 organ(s), highest expression level in putamen

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P28482 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P28482 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004229
HPA003995
HPA005700
HPA030069

<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

Binds both upstream activators and downstream substrates in multimolecular complexes. This interaction inhibits its tyrosine-kinase activity. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with MORG1, PEA15 and MKNK2 (By similarity). MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation (By similarity). Interacts with DCC (By similarity). The phosphorylated form interacts with PML (isoform PML-4). Interacts with STYX. Interacts with CDK2AP2. Interacts with CAVIN4 (By similarity). Interacts with DUSP7; the interaction enhances DUSP7 phosphatase activity (PubMed:9788880).By similarity22 Publications
(Microbial infection) Interacts with HIV-1 Nef through its SH3 domain.1 Publication

<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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111580, 258 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P28482

Database of interacting proteins

More...DIPi		DIP-519N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P28482

Protein interaction database and analysis system

More...IntActi		P28482, 101 interactors

Molecular INTeraction database

More...MINTi		P28482

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000215832

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P28482

<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

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMEX-ray2.00A1-360[»]
1TVOX-ray2.50A1-360[»]
1WZYX-ray2.50A1-360[»]
2OJGX-ray2.00A2-360[»]
2OJIX-ray2.60A2-360[»]
2OJJX-ray2.40A2-360[»]
2Y9QX-ray1.55A1-360[»]
3D42X-ray2.46B184-191[»]
3D44X-ray1.90B184-191[»]
3I5ZX-ray2.20A1-360[»]
3I60X-ray2.50A1-360[»]
3SA0X-ray1.59A1-360[»]
3TEIX-ray2.40A1-360[»]
3W55X-ray3.00A1-360[»]
4FMQX-ray2.10A1-360[»]
4FUXX-ray2.20A1-360[»]
4FUYX-ray2.00A1-360[»]
4FV0X-ray2.10A1-360[»]
4FV1X-ray1.99A1-360[»]
4FV2X-ray2.00A1-360[»]
4FV3X-ray2.20A1-360[»]
4FV4X-ray2.50A1-360[»]
4FV5X-ray2.40A1-360[»]
4FV6X-ray2.50A1-360[»]
4FV7X-ray1.90A1-360[»]
4FV8X-ray2.00A1-360[»]
4FV9X-ray2.11A1-360[»]
4G6NX-ray2.00A1-360[»]
4G6OX-ray2.20A1-360[»]
4H3PX-ray2.30A/D1-360[»]
4H3QX-ray2.20A1-360[»]
4IZ5X-ray3.19A/B/C/D8-360[»]
4IZ7X-ray1.80A/C8-360[»]
4IZAX-ray1.93A/C8-360[»]
4N0SX-ray1.80A1-360[»]
4NIFX-ray2.15B/E1-360[»]
4O6EX-ray1.95A13-360[»]
4QP1X-ray2.70A/B1-360[»]
4QP2X-ray2.23A/B1-360[»]
4QP3X-ray2.60A/B1-360[»]
4QP4X-ray2.20A/B1-360[»]
4QP6X-ray3.10A/B1-360[»]
4QP7X-ray2.25A/B1-360[»]
4QP8X-ray2.45A/B1-360[»]
4QP9X-ray2.00A1-360[»]
4QPAX-ray2.85A/B1-360[»]
4QTAX-ray1.45A1-360[»]
4QTEX-ray1.50A1-360[»]
4XJ0X-ray2.58A/B12-360[»]
4ZXTX-ray2.00A1-360[»]
4ZZMX-ray1.89A11-360[»]
4ZZNX-ray1.33A11-360[»]
4ZZOX-ray1.63A11-360[»]
5AX3X-ray2.98A1-360[»]
5BUEX-ray2.40A2-360[»]
5BUIX-ray2.12A2-360[»]
5BUJX-ray1.85A2-360[»]
5BVDX-ray1.90A2-360[»]
5BVEX-ray2.00A2-360[»]
5BVFX-ray1.90A2-360[»]
5K4IX-ray1.76A9-360[»]
5LCJX-ray1.78A1-360[»]
5LCKX-ray1.89A1-360[»]
5NGUX-ray2.74A1-360[»]
5NHFX-ray2.14A1-360[»]
5NHHX-ray1.94A1-360[»]
5NHJX-ray2.12A1-360[»]
5NHLX-ray2.07A1-360[»]
5NHOX-ray2.24A1-360[»]
5NHPX-ray1.99A1-360[»]
5NHVX-ray2.00A1-360[»]
5V60X-ray2.18A8-360[»]
5V61X-ray2.20A8-360[»]
5V62X-ray1.90A10-360[»]
5WP1X-ray1.40A4-360[»]
6DMGX-ray2.20A11-357[»]
6G8XX-ray1.76A1-360[»]
6G91X-ray1.80A1-360[»]
6G92X-ray1.99A1-360[»]
6G93X-ray1.67A1-360[»]
6G97X-ray1.90A1-360[»]
6G9AX-ray1.91A1-360[»]
6G9DX-ray1.80A1-360[»]
6G9HX-ray1.73A1-360[»]
6G9JX-ray1.98A1-360[»]
6G9KX-ray1.94A1-360[»]
6G9MX-ray1.86A1-360[»]
6G9NX-ray1.76A1-360[»]
6GDMX-ray1.91A1-360[»]
6GDQX-ray1.86A1-360[»]
6GE0X-ray1.82A1-360[»]
6GJBX-ray1.82A1-360[»]
6GJDX-ray1.58A1-360[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P28482

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

More...SMRi		P28482

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P28482

<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>Domaini25 – 313Protein kinasePROSITE-ProRule annotationAdd BLAST289

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>Regioni105 – 108Inhibitor-binding4
Regioni153 – 154Inhibitor-binding2

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>Motifi185 – 187TXY1 Publication3
Motifi318 – 322Cytoplasmic retention motif1 Publication5
Motifi327 – 333Nuclear translocation motif1 Publication7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2 – 9Poly-Ala8

<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 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

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0660 Eukaryota
ENOG410XNY0 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156771

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233024

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG014652

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P28482

KEGG Orthology (KO)

More...KOi		K04371

Identification of Orthologs from Complete Genome Data

More...OMAi		DIYIVQC

Database of Orthologous Groups

More...OrthoDBi		953344at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P28482

TreeFam database of animal gene trees

More...TreeFami		TF105097

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008349 MAPK_ERK1/2
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01770 ERK1ERK2MAPK

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...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
PS00108 PROTEIN_KINASE_ST, 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 (2)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <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
Isoform 1 (identifier: P28482-1) [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
MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR 
        60         70         80         90        100
VAIKKISPFE HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD 
       110        120        130        140        150
VYIVQDLMET DLYKLLKTQH LSNDHICYFL YQILRGLKYI HSANVLHRDL 
       160        170        180        190        200
KPSNLLLNTT CDLKICDFGL ARVADPDHDH TGFLTEYVAT RWYRAPEIML 
       210        220        230        240        250
NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI LGILGSPSQE 
       260        270        280        290        300
DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK 
       310        320        330        340        350
RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE 
       360
TARFQPGYRS
Length:360
Mass (Da):41,390
Last modified:January 23, 2007 - v3
<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:iE85D0B2A5D2D724E
GO
Isoform 2 (identifier: P28482-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     242-285: Missing.

Show »
Length:316
Mass (Da):36,432
Checksum:i6076E1767B603945
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA77753 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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 conflicti91R → Q in CAA77752 (PubMed:1319925).Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047815242 – 285Missing in isoform 2. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M84489 mRNA Translation: AAA58459.1
Z11694 mRNA Translation: CAA77752.1
Z11695 mRNA Translation: CAA77753.1 Different initiation.
DQ399292 mRNA Translation: ABD60303.1
AP000553 Genomic DNA No translation available.
AP000554 Genomic DNA No translation available.
AP000555 Genomic DNA No translation available.
BC017832 mRNA Translation: AAH17832.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13795.1 [P28482-1]

Protein sequence database of the Protein Information Resource

More...PIRi		JQ1400

NCBI Reference Sequences

More...RefSeqi		NP_002736.3, NM_002745.4 [P28482-1]
NP_620407.1, NM_138957.3 [P28482-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.431850

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000215832; ENSP00000215832; ENSG00000100030 [P28482-1]
ENST00000398822; ENSP00000381803; ENSG00000100030 [P28482-1]
ENST00000544786; ENSP00000440842; ENSG00000100030 [P28482-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5594

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5594

UCSC genome browser

More...UCSCi		uc010gtk.2 human [P28482-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Extracellular signal-regulated kinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84489 mRNA Translation: AAA58459.1
Z11694 mRNA Translation: CAA77752.1
Z11695 mRNA Translation: CAA77753.1 Different initiation.
DQ399292 mRNA Translation: ABD60303.1
AP000553 Genomic DNA No translation available.
AP000554 Genomic DNA No translation available.
AP000555 Genomic DNA No translation available.
BC017832 mRNA Translation: AAH17832.1
CCDSiCCDS13795.1 [P28482-1]
PIRiJQ1400
RefSeqiNP_002736.3, NM_002745.4 [P28482-1]
NP_620407.1, NM_138957.3 [P28482-1]
UniGeneiHs.431850

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMEX-ray2.00A1-360[»]
1TVOX-ray2.50A1-360[»]
1WZYX-ray2.50A1-360[»]
2OJGX-ray2.00A2-360[»]
2OJIX-ray2.60A2-360[»]
2OJJX-ray2.40A2-360[»]
2Y9QX-ray1.55A1-360[»]
3D42X-ray2.46B184-191[»]
3D44X-ray1.90B184-191[»]
3I5ZX-ray2.20A1-360[»]
3I60X-ray2.50A1-360[»]
3SA0X-ray1.59A1-360[»]
3TEIX-ray2.40A1-360[»]
3W55X-ray3.00A1-360[»]
4FMQX-ray2.10A1-360[»]
4FUXX-ray2.20A1-360[»]
4FUYX-ray2.00A1-360[»]
4FV0X-ray2.10A1-360[»]
4FV1X-ray1.99A1-360[»]
4FV2X-ray2.00A1-360[»]
4FV3X-ray2.20A1-360[»]
4FV4X-ray2.50A1-360[»]
4FV5X-ray2.40A1-360[»]
4FV6X-ray2.50A1-360[»]
4FV7X-ray1.90A1-360[»]
4FV8X-ray2.00A1-360[»]
4FV9X-ray2.11A1-360[»]
4G6NX-ray2.00A1-360[»]
4G6OX-ray2.20A1-360[»]
4H3PX-ray2.30A/D1-360[»]
4H3QX-ray2.20A1-360[»]
4IZ5X-ray3.19A/B/C/D8-360[»]
4IZ7X-ray1.80A/C8-360[»]
4IZAX-ray1.93A/C8-360[»]
4N0SX-ray1.80A1-360[»]
4NIFX-ray2.15B/E1-360[»]
4O6EX-ray1.95A13-360[»]
4QP1X-ray2.70A/B1-360[»]
4QP2X-ray2.23A/B1-360[»]
4QP3X-ray2.60A/B1-360[»]
4QP4X-ray2.20A/B1-360[»]
4QP6X-ray3.10A/B1-360[»]
4QP7X-ray2.25A/B1-360[»]
4QP8X-ray2.45A/B1-360[»]
4QP9X-ray2.00A1-360[»]
4QPAX-ray2.85A/B1-360[»]
4QTAX-ray1.45A1-360[»]
4QTEX-ray1.50A1-360[»]
4XJ0X-ray2.58A/B12-360[»]
4ZXTX-ray2.00A1-360[»]
4ZZMX-ray1.89A11-360[»]
4ZZNX-ray1.33A11-360[»]
4ZZOX-ray1.63A11-360[»]
5AX3X-ray2.98A1-360[»]
5BUEX-ray2.40A2-360[»]
5BUIX-ray2.12A2-360[»]
5BUJX-ray1.85A2-360[»]
5BVDX-ray1.90A2-360[»]
5BVEX-ray2.00A2-360[»]
5BVFX-ray1.90A2-360[»]
5K4IX-ray1.76A9-360[»]
5LCJX-ray1.78A1-360[»]
5LCKX-ray1.89A1-360[»]
5NGUX-ray2.74A1-360[»]
5NHFX-ray2.14A1-360[»]
5NHHX-ray1.94A1-360[»]
5NHJX-ray2.12A1-360[»]
5NHLX-ray2.07A1-360[»]
5NHOX-ray2.24A1-360[»]
5NHPX-ray1.99A1-360[»]
5NHVX-ray2.00A1-360[»]
5V60X-ray2.18A8-360[»]
5V61X-ray2.20A8-360[»]
5V62X-ray1.90A10-360[»]
5WP1X-ray1.40A4-360[»]
6DMGX-ray2.20A11-357[»]
6G8XX-ray1.76A1-360[»]
6G91X-ray1.80A1-360[»]
6G92X-ray1.99A1-360[»]
6G93X-ray1.67A1-360[»]
6G97X-ray1.90A1-360[»]
6G9AX-ray1.91A1-360[»]
6G9DX-ray1.80A1-360[»]
6G9HX-ray1.73A1-360[»]
6G9JX-ray1.98A1-360[»]
6G9KX-ray1.94A1-360[»]
6G9MX-ray1.86A1-360[»]
6G9NX-ray1.76A1-360[»]
6GDMX-ray1.91A1-360[»]
6GDQX-ray1.86A1-360[»]
6GE0X-ray1.82A1-360[»]
6GJBX-ray1.82A1-360[»]
6GJDX-ray1.58A1-360[»]
ProteinModelPortaliP28482
SMRiP28482
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111580, 258 interactors
CORUMiP28482
DIPiDIP-519N
ELMiP28482
IntActiP28482, 101 interactors
MINTiP28482
STRINGi9606.ENSP00000215832

Chemistry databases

BindingDBiP28482
ChEMBLiCHEMBL4040
DrugBankiDB07264 (S)-N-(1-(3-CHLORO-4-FLUOROPHENYL)-2-HYDROXYETHYL)-4-(4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL)-1H-PYRROLE-2-CARBOXAMIDE
DB08521 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE
DB08513 [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID
DB01169 Arsenic trioxide
DB01064 Isoprenaline
DB07010 N-BENZYL-4-[4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL]-1H-PYRROLE-2-CARBOXAMIDE
DB02116 Olomoucine
DB02482 Phosphonothreonine
DB02733 Purvalanol
DB04338 SB220025
DB11120 Turpentine
GuidetoPHARMACOLOGYi1495

Protein family/group databases

MoonDBiP28482 Predicted
MoonProtiP28482

PTM databases

iPTMnetiP28482
PhosphoSitePlusiP28482
SwissPalmiP28482

Polymorphism and mutation databases

BioMutaiMAPK1
DMDMi119554

2D gel databases

OGPiP28482

Proteomic databases

EPDiP28482
jPOSTiP28482
PaxDbiP28482
PeptideAtlasiP28482
PRIDEiP28482
ProteomicsDBi54488

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5594
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215832; ENSP00000215832; ENSG00000100030 [P28482-1]
ENST00000398822; ENSP00000381803; ENSG00000100030 [P28482-1]
ENST00000544786; ENSP00000440842; ENSG00000100030 [P28482-2]
GeneIDi5594
KEGGihsa:5594
UCSCiuc010gtk.2 human [P28482-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5594
DisGeNETi5594
EuPathDBiHostDB:ENSG00000100030.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		MAPK1
HGNCiHGNC:6871 MAPK1
HPAiCAB004229
HPA003995
HPA005700
HPA030069
MalaCardsiMAPK1
MIMi176948 gene
neXtProtiNX_P28482
OpenTargetsiENSG00000100030
Orphaneti261330 Distal 22q11.2 microdeletion syndrome
PharmGKBiPA30616

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0660 Eukaryota
ENOG410XNY0 LUCA
GeneTreeiENSGT00940000156771
HOGENOMiHOG000233024
HOVERGENiHBG014652
InParanoidiP28482
KOiK04371
OMAiDIYIVQC
OrthoDBi953344at2759
PhylomeDBiP28482
TreeFamiTF105097

Enzyme and pathway databases

BRENDAi2.7.11.24 2681
ReactomeiR-HSA-111995 phospho-PLA2 pathway
R-HSA-112409 RAF-independent MAPK1/3 activation
R-HSA-112411 MAPK1 (ERK2) activation
R-HSA-1295596 Spry regulation of FGF signaling
R-HSA-162658 Golgi Cisternae Pericentriolar Stack Reorganization
R-HSA-170968 Frs2-mediated activation
R-HSA-198753 ERK/MAPK targets
R-HSA-202670 ERKs are inactivated
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-437239 Recycling pathway of L1
R-HSA-444257 RSK activation
R-HSA-445144 Signal transduction by L1
R-HSA-450341 Activation of the AP-1 family of transcription factors
R-HSA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5654727 Negative regulation of FGFR2 signaling
R-HSA-5654732 Negative regulation of FGFR3 signaling
R-HSA-5654733 Negative regulation of FGFR4 signaling
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5668599 RHO GTPases Activate NADPH Oxidases
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5674499 Negative feedback regulation of MAPK pathway
R-HSA-5675221 Negative regulation of MAPK pathway
R-HSA-6798695 Neutrophil degranulation
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-74749 Signal attenuation
R-HSA-879415 Advanced glycosylation endproduct receptor signaling
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK
R-HSA-8939211 ESR-mediated signaling
R-HSA-8940973 RUNX2 regulates osteoblast differentiation
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-9627069 Regulation of the apoptosome activity
R-HSA-982772 Growth hormone receptor signaling
SignaLinkiP28482
SIGNORiP28482

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		MAPK1 human
EvolutionaryTraceiP28482

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MAPK1

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

More...GenomeRNAii		5594

Protein Ontology

More...PROi		PR:P28482

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000100030 Expressed in 241 organ(s), highest expression level in putamen
ExpressionAtlasiP28482 baseline and differential
GenevisibleiP28482 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008349 MAPK_ERK1/2
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PRINTSiPR01770 ERK1ERK2MAPK
SMARTiView protein in SMART
SM00220 S_TKc, 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
PS00108 PROTEIN_KINASE_ST, 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 nameiMK01_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: P28482
Secondary accession number(s): A8CZ64
<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: December 1, 1992
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 222 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, 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 chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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