MAPK1

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

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.

Cofactorⁱ

Mg²⁺By similarity

Enzyme 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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	54	ATPPROSITE-ProRule annotation	1
Binding siteⁱ	54	Inhibitor6 Publications	1
Binding siteⁱ	108	Inhibitor; via amide nitrogen and carbonyl oxygen6 Publications	1
Binding siteⁱ	114	Inhibitor6 Publications	1
Active siteⁱ	149	Proton acceptorPROSITE-ProRule annotation	1
Binding siteⁱ	154	Inhibitor6 Publications	1
Binding siteⁱ	166	Inhibitor6 Publications	1
Binding siteⁱ	167	Inhibitor6 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	31 – 39	ATPPROSITE-ProRule annotation		9
DNA bindingⁱ	259 – 277	Add BLAST		19

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
DNA binding Source: UniProtKB-KW
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16627622
- 26267534
kinase activity Source: Reactome
MAP kinase activity Source: GO_Central
MAP kinase kinase activity Source: Ensembl
mitogen-activated protein kinase kinase kinase binding Source: Ensembl
phosphatase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19494114
phosphotyrosine residue binding Source: Ensembl
protein serine/threonine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 18794356
RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB
transcription factor binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of MAPK activity Source: Reactome
apoptotic process
Source: ProtInc
Traceable author statementⁱ
- 10958679
axon guidance Source: Reactome
B cell receptor signaling pathway Source: Ensembl
Bergmann glial cell differentiation Source: Ensembl
cardiac neural crest cell development involved in heart development Source: Ensembl
caveolin-mediated endocytosis
Source: UniProtKB
Traceable author statementⁱ
- 19565474
cell cycle Source: UniProtKB-KW
cellular response to amino acid starvation
Source: CAFA
Inferred from direct assayⁱ
- 11096076
cellular response to cadmium ion
Source: CAFA
Inferred from mutant phenotypeⁱ
- 26514923
cellular response to DNA damage stimulus Source: Ensembl
cellular response to dopamine
Source: CAFA
Inferred from mutant phenotypeⁱ
- 24136195
cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: Ensembl
cellular response to reactive oxygen species
Source: CAFA
Inferred from mutant phenotypeⁱ
- 26514923
cellular response to tumor necrosis factor Source: Ensembl
chemical synaptic transmission
Source: ProtInc
Traceable author statementⁱ
- 10051431
chemotaxis
Source: ProtInc
Traceable author statementⁱ
- 10706854
cytosine metabolic process Source: Ensembl
diadenosine tetraphosphate biosynthetic process Source: Ensembl
ERBB signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 15133037
ERK1 and ERK2 cascade
Source: UniProtKB
Inferred from direct assayⁱ
- 16314496
face development Source: Ensembl
Fc-epsilon receptor signaling pathway Source: Reactome
Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
fibroblast growth factor receptor signaling pathway Source: Reactome
labyrinthine layer blood vessel development Source: Ensembl
learning or memory
Source: ARUK-UCL
Non-traceable author statementⁱ
- 11404397
lipopolysaccharide-mediated signaling pathway Source: Ensembl
long-term synaptic potentiation Source: Ensembl
lung morphogenesis Source: Ensembl
mammary gland epithelial cell proliferation Source: Ensembl
MAPK cascade Source: Reactome
negative regulation of cell differentiation Source: Ensembl
neutrophil degranulation Source: Reactome
outer ear morphogenesis Source: Ensembl
peptidyl-serine phosphorylation
Source: BHF-UCL
Inferred from direct assayⁱ
- 15850461
peptidyl-threonine phosphorylation Source: UniProtKB
platelet activation Source: Reactome
positive regulation of cell migration Source: Ensembl
positive regulation of cell proliferation Source: Ensembl
positive regulation of gene expression
Source: CAFA
Inferred from mutant phenotypeⁱ
- 24136195
positive regulation of peptidyl-threonine phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 16314496
positive regulation of protein import into nucleus, translocation Source: Ensembl
positive regulation of telomerase activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 21531765
positive regulation of telomere capping
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 21531765
positive regulation of telomere maintenance via telomerase
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 21531765
positive regulation of transcription, DNA-templated Source: Ensembl
positive regulation of translation Source: Ensembl
protein phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 23184662
regulation of cellular pH Source: Ensembl
regulation of cellular response to heat Source: Reactome
regulation of cytoskeleton organization
Source: UniProtKB
Traceable author statementⁱ
- 19565474
regulation of DNA binding transcription factor activity Source: Reactome
regulation of early endosome to late endosome transport
Source: UniProtKB
Traceable author statementⁱ
- 19565474
regulation of Golgi inheritance
Source: UniProtKB
Traceable author statementⁱ
- 19565474
regulation of ossification Source: Ensembl
regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
regulation of protein stability Source: UniProtKB
regulation of stress-activated MAPK cascade
Source: UniProtKB
Traceable author statementⁱ
- 19565474
response to epidermal growth factor
Source: UniProtKB
Inferred from direct assayⁱ
- 18794356
response to estrogen Source: Ensembl
response to exogenous dsRNA Source: Ensembl
response to nicotine Source: ARUK-UCL
sensory perception of pain Source: Ensembl
signal transduction
Source: ProtInc
Traceable author statementⁱ
- 1540184
stress-activated MAPK cascade
Source: CAFA
Inferred from direct assayⁱ
- 11096076
T cell receptor signaling pathway Source: Ensembl
thymus development Source: Ensembl
thyroid gland development Source: Ensembl
trachea formation Source: Ensembl
transcription, DNA-templated Source: UniProtKB-KW
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Kinase, Repressor, Serine/threonine-protein kinase, Transferase
Biological process	Apoptosis, Cell cycle, Host-virus interaction, Transcription, Transcription regulation
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.11.24 2681
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-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-442742 CREB phosphorylation through the activation of Ras 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-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-982772 Growth hormone receptor signaling
SignaLinkⁱ	P28482
SIGNORⁱ	P28482

Protein family/group databases

MoonDBⁱ	P28482 Predicted
MoonProtⁱ	P28482

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:MAPK1 Synonyms:ERK2, PRKM1, PRKM2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000100030.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6871 MAPK1
MIMⁱ	176948 gene
neXtProtⁱ	NX_P28482

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	54	K → R: Does not inhibit interaction with MAP2K1. 1 Publication	1
Mutagenesisⁱ	176 – 179	Missing : Inhibits homodimerization and interaction with TPR. 1 Publication	4
Mutagenesisⁱ	185	T → A: Inhibits interaction with TPR; when associated with A-187. 1 Publication	1
Mutagenesisⁱ	187	Y → A: Inhibits interaction with TPR; when associated with A-185. 1 Publication	1
Mutagenesisⁱ	234	L → A: Inhibits interaction with TPR. 1 Publication	1
Mutagenesisⁱ	318	D → A: Loss of dephosphorylation by PTPRJ. 2 Publications	1
Mutagenesisⁱ	318	D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-321. 2 Publications	1
Mutagenesisⁱ	321	D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-318. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5594
MalaCards human disease database More...MalaCardsⁱ	MAPK1
Open Targets More...OpenTargetsⁱ	ENSG00000100030
Orphanetⁱ	261330 Distal 22q11.2 microdeletion syndrome
PharmGKBⁱ	PA30616

Chemistry databases

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

BioMutaⁱ	MAPK1
DMDMⁱ	119554

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources1 Publication
ChainⁱPRO_0000186247	2 – 360	Mitogen-activated protein kinase 1Add BLAST		359

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources1 Publication	1
Modified residueⁱ	29	Phosphoserine; by SGK11 Publication	1
Modified residueⁱ	185	Phosphothreonine; by MAP2K1 and MAP2K2Combined sources	1
Modified residueⁱ	187	Phosphotyrosine; by MAP2K1 and MAP2K2Combined sources2 Publications	1
Modified residueⁱ	190	Phosphothreonine; by autocatalysis1 Publication	1
Modified residueⁱ	246	Phosphoserine1 Publication	1
Modified residueⁱ	248	Phosphoserine1 Publication	1
Modified residueⁱ	284	PhosphoserineCombined sources	1

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

EPDⁱ	P28482
PaxDbⁱ	P28482
PeptideAtlas More...PeptideAtlasⁱ	P28482
PRIDEⁱ	P28482
ProteomicsDBⁱ	54488

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	P28482

OGPⁱ

P28482

PTM databases

iPTMnetⁱ	P28482
PhosphoSitePlusⁱ	P28482
SwissPalmⁱ	P28482

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000100030
CleanExⁱ	HS_MAPK1
ExpressionAtlasⁱ	P28482 baseline and differential
Genevisibleⁱ	P28482 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004229 HPA003995 HPA005700 HPA030069

HPAⁱ

CAB004229
HPA003995
HPA005700
HPA030069

Interactionⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-959949,EBI-959949
ARRB2	P32121	3	EBI-959949,EBI-714559
BCL2	P10415	2	EBI-959949,EBI-77694
BLVRA	P53004	2	EBI-959949,EBI-7410441
cic	Q9U1H0	2	EBI-959949,EBI-98330	From Drosophila melanogaster.
COPS6	Q7L5N1	2	EBI-959949,EBI-486838
DUSP1	P28562	3	EBI-959949,EBI-975493
Dusp2	Q05922	2	EBI-959949,EBI-7898692	From Mus musculus.
DUSP4	Q13115	3	EBI-959949,EBI-6591081
DUSP5	Q16690	4	EBI-959949,EBI-7487376
ETS1	P14921	3	EBI-959949,EBI-913209
LCK	P06239	2	EBI-959949,EBI-1348
MAP2K1	Q02750	2	EBI-959949,EBI-492564
MAPK14	Q16539-3	5	EBI-959949,EBI-6932370
MAPK3	P27361	3	EBI-959949,EBI-73995
MBP	P02687	2	EBI-959949,EBI-908215	From Bos taurus.
MKNK1	Q9BUB5	4	EBI-959949,EBI-73837
PEA15	Q15121	3	EBI-959949,EBI-714410
PPM1A	P35813	19	EBI-959949,EBI-989143
PTPN7	P35236	6	EBI-959949,EBI-2265723
PTPRJ	Q12913	7	EBI-959949,EBI-2264500
PTPRR	Q15256	3	EBI-959949,EBI-2265659
RPS6KA2	Q15349	6	EBI-959949,EBI-1384149
RPS6KA3	P51812	3	EBI-959949,EBI-1046616
SHC1	P29353-2	4	EBI-959949,EBI-1000553
U24	Q69559	2	EBI-959949,EBI-8015758	From Human herpesvirus 6A (strain Uganda-1102).
YBX1	P67809	2	EBI-959949,EBI-354065
YBX3	P16989	2	EBI-959949,EBI-358193

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GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16627622
- 26267534
mitogen-activated protein kinase kinase kinase binding Source: Ensembl
phosphatase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19494114
phosphotyrosine residue binding Source: Ensembl
transcription factor binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111580, 249 interactors
CORUMⁱ	P28482
Database of interacting proteins More...DIPⁱ	DIP-519N
ELMⁱ	P28482
IntActⁱ	P28482, 108 interactors
Molecular INTeraction database More...MINTⁱ	P28482
STRINGⁱ	9606.ENSP00000215832

Chemistry databases

BindingDBⁱ

P28482

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	12 – 14	Combined sources	3
Beta strandⁱ	17 – 19	Combined sources	3
Turnⁱ	22 – 24	Combined sources	3
Beta strandⁱ	25 – 34	Combined sources	10
Beta strandⁱ	37 – 44	Combined sources	8
Turnⁱ	45 – 48	Combined sources	4
Beta strandⁱ	49 – 56	Combined sources	8
Beta strandⁱ	59 – 61	Combined sources	3
Helixⁱ	62 – 77	Combined sources	16
Beta strandⁱ	81 – 83	Combined sources	3
Beta strandⁱ	88 – 90	Combined sources	3
Turnⁱ	95 – 97	Combined sources	3
Beta strandⁱ	101 – 106	Combined sources	6
Beta strandⁱ	109 – 111	Combined sources	3
Helixⁱ	112 – 118	Combined sources	7
Helixⁱ	123 – 142	Combined sources	20
Helixⁱ	152 – 154	Combined sources	3
Beta strandⁱ	155 – 157	Combined sources	3
Turnⁱ	159 – 161	Combined sources	3
Beta strandⁱ	163 – 165	Combined sources	3
Helixⁱ	168 – 170	Combined sources	3
Helixⁱ	176 – 178	Combined sources	3
Turnⁱ	181 – 185	Combined sources	5
Helixⁱ	191 – 193	Combined sources	3
Helixⁱ	196 – 200	Combined sources	5
Beta strandⁱ	201 – 203	Combined sources	3
Helixⁱ	208 – 223	Combined sources	16
Helixⁱ	235 – 244	Combined sources	10
Helixⁱ	249 – 253	Combined sources	5
Helixⁱ	258 – 265	Combined sources	8
Helixⁱ	275 – 278	Combined sources	4
Beta strandⁱ	280 – 282	Combined sources	3
Helixⁱ	284 – 293	Combined sources	10
Turnⁱ	298 – 300	Combined sources	3
Helixⁱ	304 – 308	Combined sources	5
Helixⁱ	311 – 313	Combined sources	3
Turnⁱ	314 – 316	Combined sources	3
Helixⁱ	319 – 321	Combined sources	3
Helixⁱ	331 – 334	Combined sources	4
Helixⁱ	335 – 337	Combined sources	3
Helixⁱ	340 – 351	Combined sources	12
Helixⁱ	352 – 354	Combined sources	3
Turnⁱ	356 – 358	Combined sources	3

3D structure databases

ProteinModelPortalⁱ	P28482
SMRⁱ	P28482
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P28482

EvolutionaryTraceⁱ

P28482

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	25 – 313	Protein kinasePROSITE-ProRule annotationAdd BLAST		289

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	105 – 108	Inhibitor-binding		4
Regionⁱ	153 – 154	Inhibitor-binding		2

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	185 – 187	TXY	3
Motifⁱ	318 – 322	Cytoplasmic retention motif	5
Motifⁱ	327 – 333	Nuclear translocation motif	7

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	2 – 9	Poly-Ala		8

Domainⁱ

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG0660 Eukaryota ENOG410XNY0 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144035
HOGENOMⁱ	HOG000233024
HOVERGENⁱ	HBG014652
InParanoidⁱ	P28482
KEGG Orthology (KO) More...KOⁱ	K04371
OMAⁱ	MEKCLTF
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G08QL
PhylomeDBⁱ	P28482
TreeFamⁱ	TF105097

Family and domain databases

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
PRINTSⁱ	PR01770 ERK1ERK2MAPK
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
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

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: P28482-1) [UniParc]FASTA Add 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

Checksum:ⁱE85D0B2A5D2D724E

GO

Isoform 2 (identifier: P28482-2) [UniParc]FASTA Add to basket

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

« 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 LALDLLDKML 
       260        270        280        290        300
TFNPHKRIEV EQALAHPYLE QYYDPSDEPI AEAPFKFDME LDDLPKEKLK 
       310 
ELIFEETARF QPGYRS

Show »

Length:316

Mass (Da):36,432

Checksum:ⁱ6076E1767B603945

GO

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	91	R → Q in CAA77752 (PubMed:1319925).Curated		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_047815	242 – 285	Missing in isoform 2. 1 PublicationAdd BLAST		44

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13795.1 [P28482-1]
PIRⁱ	JQ1400
NCBI Reference Sequences More...RefSeqⁱ	NP_002736.3, NM_002745.4 [P28482-1] NP_620407.1, NM_138957.3 [P28482-1]
UniGeneⁱ	Hs.431850

Genome annotation databases

Ensemblⁱ	ENST00000215832; ENSP00000215832; ENSG00000100030 [P28482-1] ENST00000398822; ENSP00000381803; ENSG00000100030 [P28482-1] ENST00000544786; ENSP00000440842; ENSG00000100030 [P28482-2]
GeneIDⁱ	5594
KEGGⁱ	hsa:5594
UCSC genome browser More...UCSCⁱ	uc010gtk.2 human [P28482-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P28482	Mitogen-activated protein kinase		HUMAN		360
Mitogen-activated protein kinase		PANTR		360
Mitogen-activated protein kinase		CALJA		360
Mitogen-activated protein kinase		PROCO		360
Mitogen-activated protein kinase		MACMU		360
+8
P28482-2	Mitogen-activated protein kinase		PANTR		316
Mitogen-activated protein kinase		PROCO		316
Mitogen-activated protein kinase		MACMU		316
Mitogen-activated protein kinase		CALJA		316
Mitogen-activated protein kinase		Cebus capucinus imitator		316
+3

Protein	Similar proteins		Species	Score	Length
P28482	Mitogen-activated protein kinase		HUMAN		360
Mitogen-activated protein kinase		PANTR		360
Mitogen-activated protein kinase		CALJA		360
Mitogen-activated protein kinase		PROCO		360
Mitogen-activated protein kinase		MACMU		360
+8
P28482-2	Mitogen-activated protein kinase		PANTR		316
Mitogen-activated protein kinase		PROCO		316
Mitogen-activated protein kinase		MACMU		316
Mitogen-activated protein kinase		CALJA		316
Mitogen-activated protein kinase		Cebus capucinus imitator		316
+7

Protein	Similar proteins		Species	Score	Length
P28482	Mitogen-activated protein kinase		HUMAN		360
Mitogen-activated protein kinase		PANTR		360
Mitogen-activated protein kinase		CALJA		360
Mitogen-activated protein kinase		PROCO		360
Mitogen-activated protein kinase		MACMU		360
+23
P28482-2	Mitogen-activated protein kinase		ICTTR		361
Mitogen-activated protein kinase		PANTR		316
Mitogen-activated protein kinase		PROCO		316
Mitogen-activated protein kinase		MACMU		316
Mitogen-activated protein kinase		CALJA		316
+18

Cross-referencesⁱ

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13795.1 [P28482-1]
PIRⁱ	JQ1400
NCBI Reference Sequences More...RefSeqⁱ	NP_002736.3, NM_002745.4 [P28482-1] NP_620407.1, NM_138957.3 [P28482-1]
UniGeneⁱ	Hs.431850

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1PME	X-ray	2.00	A	1-360	[»]
	1TVO	X-ray	2.50	A	1-360	[»]
	1WZY	X-ray	2.50	A	1-360	[»]
	2OJG	X-ray	2.00	A	2-360	[»]
	2OJI	X-ray	2.60	A	2-360	[»]
	2OJJ	X-ray	2.40	A	2-360	[»]
	2Y9Q	X-ray	1.55	A	1-360	[»]
	3D42	X-ray	2.46	B	184-191	[»]
	3D44	X-ray	1.90	B	184-191	[»]
	3I5Z	X-ray	2.20	A	1-360	[»]
	3I60	X-ray	2.50	A	1-360	[»]
	3SA0	X-ray	1.59	A	1-360	[»]
	3TEI	X-ray	2.40	A	1-360	[»]
	3W55	X-ray	3.00	A	1-360	[»]
	4FMQ	X-ray	2.10	A	1-360	[»]
	4FUX	X-ray	2.20	A	1-360	[»]
	4FUY	X-ray	2.00	A	1-360	[»]
	4FV0	X-ray	2.10	A	1-360	[»]
	4FV1	X-ray	1.99	A	1-360	[»]
	4FV2	X-ray	2.00	A	1-360	[»]
	4FV3	X-ray	2.20	A	1-360	[»]
	4FV4	X-ray	2.50	A	1-360	[»]
	4FV5	X-ray	2.40	A	1-360	[»]
	4FV6	X-ray	2.50	A	1-360	[»]
	4FV7	X-ray	1.90	A	1-360	[»]
	4FV8	X-ray	2.00	A	1-360	[»]
	4FV9	X-ray	2.11	A	1-360	[»]
	4G6N	X-ray	2.00	A	1-360	[»]
	4G6O	X-ray	2.20	A	1-360	[»]
	4H3P	X-ray	2.30	A/D	1-360	[»]
	4H3Q	X-ray	2.20	A	1-360	[»]
	4IZ5	X-ray	3.19	A/B/C/D	8-360	[»]
	4IZ7	X-ray	1.80	A/C	8-360	[»]
	4IZA	X-ray	1.93	A/C	8-360	[»]
	4N0S	X-ray	1.80	A	1-360	[»]
	4NIF	X-ray	2.15	B/E	1-360	[»]
	4O6E	X-ray	1.95	A	13-360	[»]
	4QP1	X-ray	2.70	A/B	1-360	[»]
	4QP2	X-ray	2.23	A/B	1-360	[»]
	4QP3	X-ray	2.60	A/B	1-360	[»]
	4QP4	X-ray	2.20	A/B	1-360	[»]
	4QP6	X-ray	3.10	A/B	1-360	[»]
	4QP7	X-ray	2.25	A/B	1-360	[»]
	4QP8	X-ray	2.45	A/B	1-360	[»]
	4QP9	X-ray	2.00	A	1-360	[»]
	4QPA	X-ray	2.85	A/B	1-360	[»]
	4QTA	X-ray	1.45	A	1-360	[»]
	4QTE	X-ray	1.50	A	1-360	[»]
	4XJ0	X-ray	2.58	A/B	12-360	[»]
	4ZXT	X-ray	2.00	A	1-360	[»]
	4ZZM	X-ray	1.89	A	11-360	[»]
	4ZZN	X-ray	1.33	A	11-360	[»]
	4ZZO	X-ray	1.63	A	11-360	[»]
	5AX3	X-ray	2.98	A	1-360	[»]
	5BUE	X-ray	2.40	A	2-360	[»]
	5BUI	X-ray	2.12	A	2-360	[»]
	5BUJ	X-ray	1.85	A	2-360	[»]
	5BVD	X-ray	1.90	A	2-360	[»]
	5BVE	X-ray	2.00	A	2-360	[»]
	5BVF	X-ray	1.90	A	2-360	[»]
	5K4I	X-ray	1.76	A	9-360	[»]
	5LCJ	X-ray	1.78	A	1-360	[»]
	5LCK	X-ray	1.89	A	1-360	[»]
5NGU	X-ray	2.74	A	1-360	[»]
5NHF	X-ray	2.14	A	1-360	[»]
5NHH	X-ray	1.94	A	1-360	[»]
5NHJ	X-ray	2.12	A	1-360	[»]
5NHL	X-ray	2.07	A	1-360	[»]
5NHO	X-ray	2.24	A	1-360	[»]
5NHP	X-ray	1.99	A	1-360	[»]
5NHV	X-ray	2.00	A	1-360	[»]
5V60	X-ray	2.18	A	8-360	[»]
5V61	X-ray	2.20	A	8-360	[»]
5V62	X-ray	1.90	A	10-360	[»]
6G8X	X-ray	1.76	A	1-360	[»]
6G91	X-ray	1.80	A	1-360	[»]
6G92	X-ray	1.99	A	1-360	[»]
6G93	X-ray	1.67	A	1-360	[»]
6G97	X-ray	1.90	A	1-360	[»]
6G9A	X-ray	1.91	A	1-360	[»]
6G9D	X-ray	1.80	A	1-360	[»]
6G9H	X-ray	1.73	A	1-360	[»]
6G9J	X-ray	1.98	A	1-360	[»]
6G9K	X-ray	1.94	A	1-360	[»]
6G9M	X-ray	1.86	A	1-360	[»]
6G9N	X-ray	1.76	A	1-360	[»]
6GDM	X-ray	1.91	A	1-360	[»]
6GDQ	X-ray	1.86	A	1-360	[»]
6GE0	X-ray	1.82	A	1-360	[»]
ProteinModelPortalⁱ	P28482
SMRⁱ	P28482
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111580, 249 interactors
CORUMⁱ	P28482
Database of interacting proteins More...DIPⁱ	DIP-519N
ELMⁱ	P28482
IntActⁱ	P28482, 108 interactors
Molecular INTeraction database More...MINTⁱ	P28482
STRINGⁱ	9606.ENSP00000215832

Chemistry databases

BindingDBⁱ	P28482
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

Protein family/group databases

MoonDBⁱ	P28482 Predicted
MoonProtⁱ	P28482

PTM databases

iPTMnetⁱ	P28482
PhosphoSitePlusⁱ	P28482
SwissPalmⁱ	P28482

Polymorphism and mutation databases

BioMutaⁱ	MAPK1
DMDMⁱ	119554

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	P28482

OGPⁱ

P28482

Proteomic databases

EPDⁱ	P28482
PaxDbⁱ	P28482
PeptideAtlas More...PeptideAtlasⁱ	P28482
PRIDEⁱ	P28482
ProteomicsDBⁱ	54488

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5594
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000215832; ENSP00000215832; ENSG00000100030 [P28482-1] ENST00000398822; ENSP00000381803; ENSG00000100030 [P28482-1] ENST00000544786; ENSP00000440842; ENSG00000100030 [P28482-2]
GeneIDⁱ	5594
KEGGⁱ	hsa:5594
UCSC genome browser More...UCSCⁱ	uc010gtk.2 human [P28482-1]

Organism-specific databases

CTDⁱ	5594
DisGeNET More...DisGeNETⁱ	5594
EuPathDBⁱ	HostDB:ENSG00000100030.14
GeneCardsⁱ	MAPK1
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6871 MAPK1
Human Protein Atlas More...HPAⁱ	CAB004229 HPA003995 HPA005700 HPA030069
MalaCards human disease database More...MalaCardsⁱ	MAPK1
MIMⁱ	176948 gene
neXtProtⁱ	NX_P28482
Open Targets More...OpenTargetsⁱ	ENSG00000100030
Orphanetⁱ	261330 Distal 22q11.2 microdeletion syndrome
PharmGKBⁱ	PA30616
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0660 Eukaryota ENOG410XNY0 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144035
HOGENOMⁱ	HOG000233024
HOVERGENⁱ	HBG014652
InParanoidⁱ	P28482
KEGG Orthology (KO) More...KOⁱ	K04371
OMAⁱ	MEKCLTF
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G08QL
PhylomeDBⁱ	P28482
TreeFamⁱ	TF105097

Enzyme and pathway databases

BRENDAⁱ	2.7.11.24 2681
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-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-442742 CREB phosphorylation through the activation of Ras 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-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-982772 Growth hormone receptor signaling
SignaLinkⁱ	P28482
SIGNORⁱ	P28482

Miscellaneous databases

ChiTaRSⁱ	MAPK1 human
EvolutionaryTraceⁱ	P28482
GeneWikiⁱ	MAPK1
GenomeRNAiⁱ	5594
Protein Ontology More...PROⁱ	PR:P28482
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000100030
CleanExⁱ	HS_MAPK1
ExpressionAtlasⁱ	P28482 baseline and differential
Genevisibleⁱ	P28482 HS

Family and domain databases

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
PRINTSⁱ	PR01770 ERK1ERK2MAPK
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MK01_HUMAN
Accessionⁱ	P28482Primary (citable) accession number: P28482 Secondary accession number(s): A8CZ64
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
	Last sequence update:	January 23, 2007
	Last modified:	July 18, 2018
	This is version 216 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human and mouse protein kinases
Human and mouse protein kinases: classification and index
SIMILARITY comments
Index of protein domains and families

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Supporting data

UniProtKB - P28482 (MK01_HUMAN)

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Mitogen-activated protein kinase 1

Select a section on the left to see content.

<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

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

Sites

Regions

<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

<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 - Biological processi

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

Nucleus

Cytoskeleton

Other locations

Cytoskeleton

Cytosol

Endosome

Extracellular region or secreted

Golgi apparatus

Lysosome

Mitochondrion

Nucleus

Plasma Membrane

Other locations

<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

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Proteomic databases

2D gel databases

PTM databases

<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

Organism-specific databases

<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>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

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Region

Motif

Compositional bias

<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

Phylogenomic databases

Family and domain databases

<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

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

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Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ