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UniProtKB - P36507 (MP2K2_HUMAN)

Entry version 228 (02 Dec 2020)
Sequence version 1 (01 Jun 1994)
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Protein

Dual specificity mitogen-activated protein kinase kinase 2

Gene

MAP2K2

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

Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei101ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei194Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi78 – 86ATPPROSITE-ProRule annotation9

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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.12.2, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P36507

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-112411, MAPK1 (ERK2) activation
R-HSA-170968, Frs2-mediated activation
R-HSA-445144, Signal transduction by L1
R-HSA-5210891, Uptake and function of anthrax toxins
R-HSA-5673000, RAF activation
R-HSA-5674135, MAP2K and MAPK activation
R-HSA-5674499, Negative feedback regulation of MAPK pathway
R-HSA-6802946, Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948, Signaling by high-kinase activity BRAF mutants
R-HSA-6802952, Signaling by BRAF and RAF fusions
R-HSA-6802955, Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-9649948, Signaling downstream of RAS mutants
R-HSA-9652169, Signaling by MAP2K mutants
R-HSA-9656223, Signaling by RAF1 mutants

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

More...SignaLinki		P36507

SIGNOR Signaling Network Open Resource

More...SIGNORi		P36507

<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%5Fand%5Ftaxonomy%5Fsection">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:
Dual specificity mitogen-activated protein kinase kinase 2 (EC:2.7.12.21 Publication)
Short name:
MAP kinase kinase 2
Short name:
MAPKK 2
Alternative name(s):
ERK activator kinase 2
MAPK/ERK kinase 2
Short name:
MEK 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:MAP2K2
Synonyms:MEK2, MKK2, PRKMK2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 19

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000126934.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:6842, MAP2K2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601263, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P36507

<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, Membrane

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cardiofaciocutaneous syndrome 4 (CFC4)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03509557F → C in CFC4. 1 PublicationCorresponds to variant dbSNP:rs121434497EnsemblClinVar.1
Natural variantiVAR_06978157F → V in CFC4. 1 PublicationCorresponds to variant dbSNP:rs121434498EnsemblClinVar.1
Natural variantiVAR_069782128P → Q in CFC4; results in increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs267607230EnsemblClinVar.1
Natural variantiVAR_069783134Y → H in CFC4. 1 PublicationCorresponds to variant dbSNP:rs121434499EnsemblClinVar.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Ectodermal dysplasia, Mental retardation

Organism-specific databases

DisGeNET

More...DisGeNETi		5605

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		MAP2K2

MalaCards human disease database

More...MalaCardsi		MAP2K2
MIMi615280, phenotype

Open Targets

More...OpenTargetsi		ENSG00000126934

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

More...Orphaneti		1340, Cardiofaciocutaneous syndrome
638, Neurofibromatosis-Noonan syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30587

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P36507, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2964

Drug and drug target database

More...DrugBanki		DB11967, Binimetinib
DB06616, Bosutinib
DB12010, Fostamatinib
DB11689, Selumetinib
DB08911, Trametinib

DrugCentral

More...DrugCentrali		P36507

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2063

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MAP2K2

Domain mapping of disease mutations (DMDM)

More...DMDMi		547915

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000863721 – 400Dual specificity mitogen-activated protein kinase kinase 2Add BLAST400

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 residuei1N-acetylmethionineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei222(Microbial infection) O-acetylserine; by Yersinia YopJ; alternate1 Publication1
Modified residuei222Phosphoserine; by RAF; alternate2 Publications1
Modified residuei226(Microbial infection) O-acetylserine; by Yersinia YopJ; alternate1 Publication1
Modified residuei226Phosphoserine; alternate1 Publication1
Modified residuei293PhosphoserineCombined sources1
Modified residuei295PhosphoserineCombined sources1
Modified residuei306PhosphoserineBy similarity1
Modified residuei394PhosphothreonineCombined sources1 Publication1
Modified residuei396PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

MAPKK is itself dependent on Ser/Thr phosphorylation for activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1). Phosphorylated by MAP2K1/MEK1 (By similarity).By similarity
(Microbial infection) Acetylation of Ser-222 and Ser-226 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei10 – 11Cleavage; by anthrax lethal factor2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1045
CPTAC-1543
CPTAC-811
CPTAC-812
CPTAC-813

Encyclopedia of Proteome Dynamics

More...EPDi		P36507

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P36507

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P36507

MaxQB - The MaxQuant DataBase

More...MaxQBi		P36507

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

More...PaxDbi		P36507

PeptideAtlas

More...PeptideAtlasi		P36507

PRoteomics IDEntifications database

More...PRIDEi		P36507

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55203

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00003783

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P36507

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P36507

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

More...PhosphoSitePlusi		P36507

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P36507

<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		ENSG00000126934, Expressed in testis and 245 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P36507, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P36507, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000126934, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with MORG1 (By similarity).

Interacts with SGK1 (PubMed:19447520).

Interacts with KSR1 (PubMed:10409742).

Interacts with KSR1 and BRAF; the interaction with KSR1 mediates KSR1-BRAF dimerization (PubMed:29433126).

Interacts with GLS (PubMed:22538822).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111591, 65 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P36507

Database of interacting proteins

More...DIPi		DIP-29119N

Protein interaction database and analysis system

More...IntActi		P36507, 64 interactors

Molecular INTeraction database

More...MINTi		P36507

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000262948

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P36507

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P36507, protein

<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

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P36507

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P36507

<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%5Fand%5Fdomains%5Fsection">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>Domaini72 – 369Protein kinasePROSITE-ProRule annotationAdd BLAST298

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 biasi266 – 315Pro-richAdd BLAST50

<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. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0581, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153487

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P36507

Identification of Orthologs from Complete Genome Data

More...OMAi		VEMSIGR

Database of Orthologous Groups

More...OrthoDBi		688282at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P36507

TreeFam database of animal gene trees

More...TreeFami		TF105137

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011009, Kinase-like_dom_sf
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

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
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P36507-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELELDEQQ 
        60         70         80         90        100
KKRLEAFLTQ KAKVGELKDD DFERISELGA GNGGVVTKVQ HRPSGLIMAR 
       110        120        130        140        150
KLIHLEIKPA IRNQIIRELQ VLHECNSPYI VGFYGAFYSD GEISICMEHM 
       160        170        180        190        200
DGGSLDQVLK EAKRIPEEIL GKVSIAVLRG LAYLREKHQI MHRDVKPSNI 
       210        220        230        240        250
LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMAPERLQ GTHYSVQSDI 
       260        270        280        290        300
WSMGLSLVEL AVGRYPIPPP DAKELEAIFG RPVVDGEEGE PHSISPRPRP 
       310        320        330        340        350
PGRPVSGHGM DSRPAMAIFE LLDYIVNEPP PKLPNGVFTP DFQEFVNKCL 
       360        370        380        390        400
IKNPAERADL KMLTNHTFIK RSEVEEVDFA GWLCKTLRLN QPGTPTRTAV
Length:400
Mass (Da):44,424
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3401D522515C30A5
GO

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

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G5E9C7G5E9C7_HUMAN
Dual-specificity mitogen-activated ...
MAP2K2 hCG_23544
303Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0R1B6M0R1B6_HUMAN
Dual-specificity mitogen-activated ...
MAP2K2
104Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti56A → R AA sequence (PubMed:10409742).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03509557F → C in CFC4. 1 PublicationCorresponds to variant dbSNP:rs121434497EnsemblClinVar.1
Natural variantiVAR_06978157F → V in CFC4. 1 PublicationCorresponds to variant dbSNP:rs121434498EnsemblClinVar.1
Natural variantiVAR_069782128P → Q in CFC4; results in increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs267607230EnsemblClinVar.1
Natural variantiVAR_069783134Y → H in CFC4. 1 PublicationCorresponds to variant dbSNP:rs121434499EnsemblClinVar.1

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
L11285 mRNA No translation available.
BC000471 mRNA Translation: AAH00471.1
BC018645 mRNA Translation: AAH18645.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12120.1

Protein sequence database of the Protein Information Resource

More...PIRi		A46723

NCBI Reference Sequences

More...RefSeqi		NP_109587.1, NM_030662.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000262948; ENSP00000262948; ENSG00000126934

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5605

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5605

UCSC genome browser

More...UCSCi		uc002lzk.4, human

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11285 mRNA No translation available.
BC000471 mRNA Translation: AAH00471.1
BC018645 mRNA Translation: AAH18645.1
CCDSiCCDS12120.1
PIRiA46723
RefSeqiNP_109587.1, NM_030662.3

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
1S9IX-ray3.20A/B55-400[»]
4H3QX-ray2.20B4-16[»]
SMRiP36507
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111591, 65 interactors
CORUMiP36507
DIPiDIP-29119N
IntActiP36507, 64 interactors
MINTiP36507
STRINGi9606.ENSP00000262948

Chemistry databases

BindingDBiP36507
ChEMBLiCHEMBL2964
DrugBankiDB11967, Binimetinib
DB06616, Bosutinib
DB12010, Fostamatinib
DB11689, Selumetinib
DB08911, Trametinib
DrugCentraliP36507
GuidetoPHARMACOLOGYi2063

PTM databases

iPTMnetiP36507
MetOSiteiP36507
PhosphoSitePlusiP36507
SwissPalmiP36507

Polymorphism and mutation databases

BioMutaiMAP2K2
DMDMi547915

2D gel databases

REPRODUCTION-2DPAGEiIPI00003783

Proteomic databases

CPTACiCPTAC-1045
CPTAC-1543
CPTAC-811
CPTAC-812
CPTAC-813
EPDiP36507
jPOSTiP36507
MassIVEiP36507
MaxQBiP36507
PaxDbiP36507
PeptideAtlasiP36507
PRIDEiP36507
ProteomicsDBi55203

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3543, 1338 antibodies

The DNASU plasmid repository

More...DNASUi		5605

Genome annotation databases

EnsembliENST00000262948; ENSP00000262948; ENSG00000126934
GeneIDi5605
KEGGihsa:5605
UCSCiuc002lzk.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5605
DisGeNETi5605
EuPathDBiHostDB:ENSG00000126934.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		MAP2K2
GeneReviewsiMAP2K2
HGNCiHGNC:6842, MAP2K2
HPAiENSG00000126934, Low tissue specificity
MalaCardsiMAP2K2
MIMi601263, gene
615280, phenotype
neXtProtiNX_P36507
OpenTargetsiENSG00000126934
Orphaneti1340, Cardiofaciocutaneous syndrome
638, Neurofibromatosis-Noonan syndrome
PharmGKBiPA30587

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0581, Eukaryota
GeneTreeiENSGT00940000153487
InParanoidiP36507
OMAiVEMSIGR
OrthoDBi688282at2759
PhylomeDBiP36507
TreeFamiTF105137

Enzyme and pathway databases

BRENDAi2.7.12.2, 2681
PathwayCommonsiP36507
ReactomeiR-HSA-112411, MAPK1 (ERK2) activation
R-HSA-170968, Frs2-mediated activation
R-HSA-445144, Signal transduction by L1
R-HSA-5210891, Uptake and function of anthrax toxins
R-HSA-5673000, RAF activation
R-HSA-5674135, MAP2K and MAPK activation
R-HSA-5674499, Negative feedback regulation of MAPK pathway
R-HSA-6802946, Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948, Signaling by high-kinase activity BRAF mutants
R-HSA-6802952, Signaling by BRAF and RAF fusions
R-HSA-6802955, Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-9649948, Signaling downstream of RAS mutants
R-HSA-9652169, Signaling by MAP2K mutants
R-HSA-9656223, Signaling by RAF1 mutants
SignaLinkiP36507
SIGNORiP36507

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5605, 19 hits in 871 CRISPR screens

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

More...ChiTaRSi		MAP2K2, human
EvolutionaryTraceiP36507

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MAP2K2

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

More...GenomeRNAii		5605
PharosiP36507, Tclin

Protein Ontology

More...PROi		PR:P36507
RNActiP36507, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000126934, Expressed in testis and 245 other tissues
ExpressionAtlasiP36507, baseline and differential
GenevisibleiP36507, HS

Family and domain databases

InterProiView protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiMP2K2_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: P36507
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 2, 2020
This is version 228 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
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