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Entry version 215 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Dual specificity mitogen-activated protein kinase kinase 1

Gene

MAP2K1

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

Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. 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). Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of 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.3 Publications

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Ras proteins such as HRAS mediate the activation of RAF proteins such as RAF1 or BRAF which in turn activate extracellular signal-regulated kinases (ERK) through MAPK (mitogen-activated protein kinases) and ERK kinases MAP2K1/MEK1 and MAP2K2/MEK2 (PubMed:29433126). Activation occurs through phosphorylation of Ser-218 and Ser-222 (By similarity). MAP2K1/MEK1 binds KSR1 or KSR2 releasing the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains (PubMed:29433126). This allows KSR1 or KSR2 dimerization with BRAF leading to BRAF activation and phosphorylation of MAP2K1 (PubMed:29433126). MAP2K1/MEK1 is also the target of negative feed-back regulation by its substrate kinases, such as MAPK1/ERK2. These phosphorylate MAP2K1/MEK1 on Thr-292, thereby facilitating dephosphorylation of the activating residues Ser-218 and Ser-222. Inhibited by serine/threonine phosphatase 2A (By similarity). Many inhibitors have been identified including pyrrole derivatives, TAK-733 (one of a series of 8-methylpyrido[2,3-d]pyrimidine-4,7(3H,8H)-dione derivatives), CH4987655 and RDEA119/BAY 869766 (PubMed:21310613, PubMed:20621728, PubMed:19706763, PubMed:19019675, PubMed:19161339, PubMed:18951019, PubMed:17880056, PubMed:15543157).By similarity9 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei77Inhibitor; via carbonyl oxygen8 Publications1
Binding sitei78Inhibitor; via amide nitrogen and carbonyl oxygen8 Publications1
Binding sitei97ATPPROSITE-ProRule annotation6 Publications1
Binding sitei97Inhibitor8 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei190Proton acceptorPROSITE-ProRule annotation1
Binding sitei190Inhibitor8 Publications1
Binding sitei194Inhibitor; via carbonyl oxygen8 Publications1
Binding sitei208ATPPROSITE-ProRule annotation6 Publications1
Binding sitei208Inhibitor8 Publications1
Binding sitei212Inhibitor; via amide nitrogen8 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi74 – 82ATPPROSITE-ProRule annotation6 Publications9
Nucleotide bindingi143 – 146ATPPROSITE-ProRule annotation6 Publications4
Nucleotide bindingi150 – 153ATPPROSITE-ProRule annotation6 Publications4
Nucleotide bindingi192 – 195ATPPROSITE-ProRule annotation6 Publications4

<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

GO - Biological processi

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

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.12.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-110056 MAPK3 (ERK1) 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-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
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

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

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SignaLinki
Q02750

SIGNOR Signaling Network Open Resource

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SIGNORi
Q02750

<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:
Dual specificity mitogen-activated protein kinase kinase 1 (EC:2.7.12.2)
Short name:
MAP kinase kinase 1
Short name:
MAPKK 1
Short name:
MKK1
Alternative name(s):
ERK activator kinase 1
MAPK/ERK kinase 1
Short name:
MEK 1
<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:MAP2K1
Synonyms:MEK1, PRKMK1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:6840 MAP2K1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176872 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q02750

<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

<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 3 (CFC3)2 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. Distinctive features of CFC3 include macrostomia and horizontal shape of palpebral fissures.
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_03509353F → S in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908594EnsemblClinVar.1
Natural variantiVAR_069780128G → V in CFC3. 1 PublicationCorresponds to variant dbSNP:rs730880508EnsemblClinVar.1
Natural variantiVAR_035094130Y → C in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908595EnsemblClinVar.1

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>Mutagenesisi97K → R: Loss of catalytic activity. No effect on BRAF-KSR1 or BRAF-KSR2 dimerization. 2 Publications1
Mutagenesisi150S → A: No loss of activity. 1 Publication1
Mutagenesisi212S → A: No loss of activity. 1 Publication1
Mutagenesisi218S → A: Loss of catalytic activity. No effect on BRAF-KSR1 dimerization; when associated with A-222. 2 Publications1
Mutagenesisi218S → D: No effect on BRAF-KSR1 dimerization; when associated with D-222. 1 Publication1
Mutagenesisi219M → V: Increases interaction with KSR1 and BRAF. 1 Publication1
Mutagenesisi219M → W: Increases interaction with KSR1 and BRAF; when associated with L-220. 1 Publication1
Mutagenesisi220A → L: Increases interaction with KSR1 and BRAF; when associated with w-219. 1 Publication1
Mutagenesisi221N → Y: Increases interaction with KSR1 and BRAF. 1 Publication1
Mutagenesisi222S → A: Loss of catalytic activity. No effect on BRAF-KSR1 dimerization; when associated with A-218. 2 Publications1
Mutagenesisi222S → D: No effect on BRAF-KSR1 dimerization; when associated with D-218. 1 Publication1
Mutagenesisi311F → S: Loss of interaction with BRAF and KSR1. Loss of BRAF-KSR1 dimerization. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Ectodermal dysplasia, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
5604

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

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GeneReviewsi
MAP2K1

MalaCards human disease database

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MalaCardsi
MAP2K1
MIMi615279 phenotype

Open Targets

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OpenTargetsi
ENSG00000169032

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

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Orphaneti
1340 Cardiofaciocutaneous syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30584

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q02750

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3587

Drug and drug target database

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DrugBanki
DB06892 (5S)-4,5-difluoro-6-[(2-fluoro-4-iodophenyl)imino]-N-(2-hydroxyethoxy)cyclohexa-1,3-diene-1-carboxamide
DB07046 2-[(2-chloro-4-iodophenyl)amino]-N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluorobenzamide
DB08208 2-[(4-ETHYNYL-2-FLUOROPHENYL)AMINO]-3,4-DIFLUORO-N-(2-HYDROXYETHOXY)BENZAMIDE
DB03115 5-Bromo-N-(2,3-Dihydroxypropoxy)-3,4-Difluoro-2-[(2-Fluoro-4-Iodophenyl)Amino]Benzamide
DB06616 Bosutinib
DB05239 Cobimetinib
DB02152 K-252a
DB08130 N-(5-{3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]phenyl}-1,3,4-oxadiazol-2-yl)ethane-1,2-diamine
DB07101 PD-0325901
DB08911 Trametinib

DrugCentral

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DrugCentrali
Q02750

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2062

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MAP2K1

Domain mapping of disease mutations (DMDM)

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DMDMi
400274

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000863651 – 393Dual specificity mitogen-activated protein kinase kinase 1Add BLAST393

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 residuei218Phosphoserine; by BRAF and RAF13 Publications1
Modified residuei222Phosphoserine; by BRAF and RAF12 Publications1
Modified residuei286PhosphothreonineCombined sources1
Modified residuei292Phosphothreonine; by MAPK1By similarity1
Modified residuei298Phosphoserine; by PAK1 Publication1

<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

Phosphorylation at Ser-218 and Ser-222 by MAP kinase kinase kinases (BRAF or MEKK1) positively regulates kinase activity (PubMed:29433126, PubMed:8131746). Also phosphorylated at Thr-292 by MAPK1/ERK2 and at Ser-298 by PAK (PubMed:16129686). MAPK1/ERK2 phosphorylation of Thr-292 occurs in response to cellular adhesion and leads to inhibition of Ser-298 phosphorylation by PAK (PubMed:16129686).3 Publications
Acetylation by Yersinia yopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.1 Publication

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>Sitei8 – 9Cleavage; by anthrax lethal factor2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

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CPTACi
CPTAC-808
CPTAC-809

Encyclopedia of Proteome Dynamics

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EPDi
Q02750

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q02750

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q02750

MaxQB - The MaxQuant DataBase

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MaxQBi
Q02750

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

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PaxDbi
Q02750

PeptideAtlas

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PeptideAtlasi
Q02750

PRoteomics IDEntifications database

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PRIDEi
Q02750

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
58119 [Q02750-1]
58120 [Q02750-2]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
Q02750

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q02750

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

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PhosphoSitePlusi
Q02750

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q02750

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q02750

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

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

Widely expressed, with extremely low levels in brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000169032 Expressed in 235 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q02750 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q02750 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003834
HPA026430

<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

Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3/ERK1 and RGS14 (By similarity).

Forms a heterodimer with MAP2K2/MEK2 (By similarity). Forms heterodimers with KSR2 which further dimerize to form tetramers (By similarity).

Interacts with KSR1 or KSR2 and BRAF; the interaction with KSR1 or KSR2 mediates KSR1-BRAF or KSR2-BRAF dimerization (PubMed:10409742, PubMed:29433126).

Interacts with ARBB2, LAMTOR3, MAPK1/ERK2 and RAF1 (By similarity).

Interacts with MORG1 (By similarity).

Interacts with PPARG (PubMed:17101779).

Interacts with isoform 1 of VRK2 (PubMed:20679487).

Interacts with SGK1 (PubMed:19447520).

Interacts with BIRC6/bruce (PubMed:18329369).

Interacts with KAT7; the interaction promotes KAT7 phosphorylation (By similarity).

By similarity6 Publications

(Microbial infection) Interacts with Yersinia yopJ.

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111590, 122 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q02750

Database of interacting proteins

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DIPi
DIP-201N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q02750

Protein interaction database and analysis system

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IntActi
Q02750, 76 interactors

Molecular INTeraction database

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MINTi
Q02750

STRING: functional protein association networks

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STRINGi
9606.ENSP00000302486

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q02750

<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

1393
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

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SMRi
Q02750

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q02750

<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>Domaini68 – 361Protein kinasePROSITE-ProRule annotationAdd BLAST294

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>Regioni77 – 78Inhibitor binding2
Regioni144 – 146Inhibitor binding3
Regioni208 – 212Inhibitor binding5
Regioni270 – 307RAF1-bindingBy similarityAdd BLAST38

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 biasi262 – 307Pro-richAdd BLAST46

<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 proline-rich region localized between residues 270 and 307 is important for binding to RAF1 and activation of MAP2K1/MEK1.By similarity

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0581 Eukaryota
ENOG410XQ5A LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153487

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234206

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q02750

KEGG Orthology (KO)

More...
KOi
K04368

Identification of Orthologs from Complete Genome Data

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OMAi
GSEFQDF

Database of Orthologous Groups

More...
OrthoDBi
688282at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q02750

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_length">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>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.

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

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

Isoform 1 (identifier: Q02750-1) [UniParc]FASTAAdd to basket
Also known as: MKK1a

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL
60 70 80 90 100
EAFLTQKQKV GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH
110 120 130 140 150
LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS
160 170 180 190 200
LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD VKPSNILVNS
210 220 230 240 250
RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG
260 270 280 290 300
LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLSSY
310 320 330 340 350
GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA
360 370 380 390
DLKQLMVHAF IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA AGV
Length:393
Mass (Da):43,439
Last modified:January 23, 2007 - v2
<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:i0344118FFC842D51
GO
Isoform 2 (identifier: Q02750-2) [UniParc]FASTAAdd to basket
Also known as: MKK1b

The sequence of this isoform differs from the canonical sequence as follows:
     147-172: Missing.

Show »
Length:367
Mass (Da):40,764
Checksum:i9944432D8705DEFD
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BRW9H3BRW9_HUMAN
Dual-specificity mitogen-activated ...
MAP2K1
217Annotation 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 conflicti52A → R AA sequence (PubMed:10409742).Curated1
Sequence conflicti180Missing AA sequence (PubMed:10409742).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03509353F → S in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908594EnsemblClinVar.1
Natural variantiVAR_069780128G → V in CFC3. 1 PublicationCorresponds to variant dbSNP:rs730880508EnsemblClinVar.1
Natural variantiVAR_035094130Y → C in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908595EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_040500147 – 172Missing in isoform 2. 1 PublicationAdd BLAST26

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
L05624 mRNA Translation: AAA36318.1
L11284 mRNA No translation available.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10216.1 [Q02750-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A45100

NCBI Reference Sequences

More...
RefSeqi
NP_002746.1, NM_002755.3 [Q02750-1]
XP_016877900.1, XM_017022411.1 [Q02750-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000307102; ENSP00000302486; ENSG00000169032 [Q02750-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5604

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5604

UCSC genome browser

More...
UCSCi
uc010bhq.4 human [Q02750-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05624 mRNA Translation: AAA36318.1
L11284 mRNA No translation available.
CCDSiCCDS10216.1 [Q02750-1]
PIRiA45100
RefSeqiNP_002746.1, NM_002755.3 [Q02750-1]
XP_016877900.1, XM_017022411.1 [Q02750-2]

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
1S9JX-ray2.40A62-393[»]
2P55X-ray2.80A62-393[»]
3DV3X-ray2.30A62-382[»]
3DY7X-ray2.70A62-393[»]
3E8NX-ray2.50A62-393[»]
3EQBX-ray2.62A62-393[»]
3EQCX-ray1.80A35-393[»]
3EQDX-ray2.10A35-393[»]
3EQFX-ray2.70A35-393[»]
3EQGX-ray2.50A35-393[»]
3EQHX-ray2.00A35-393[»]
3EQIX-ray1.90A35-393[»]
3MBLX-ray2.60A62-382[»]
3ORNX-ray2.80A62-393[»]
3OS3X-ray2.80A62-393[»]
3PP1X-ray2.70A62-382[»]
3SLSX-ray2.30A/B45-263[»]
A/B308-383[»]
3V01X-ray2.70A62-393[»]
3V04X-ray2.70A62-393[»]
3VVHX-ray2.00A/B/C62-393[»]
3W8QX-ray2.20A39-382[»]
3WIGX-ray2.70A62-393[»]
3ZLSX-ray2.50A37-383[»]
3ZLWX-ray2.12A37-383[»]
3ZLXX-ray2.20A37-383[»]
3ZLYX-ray2.11A37-383[»]
3ZM4X-ray2.37A37-383[»]
4AN2X-ray2.50A61-392[»]
4AN3X-ray2.10A61-392[»]
4AN9X-ray2.80A61-392[»]
4ANBX-ray2.20A61-392[»]
4ARKX-ray2.60A62-393[»]
4LMNX-ray2.80A62-393[»]
4MNEX-ray2.85A/D/E/H62-393[»]
4U7ZX-ray2.80A62-393[»]
4U80X-ray2.80A62-393[»]
4U81X-ray2.70A62-393[»]
5BX0X-ray2.93A37-383[»]
5EYMX-ray2.70A/B35-393[»]
5HZEX-ray2.40A37-383[»]
5YT3X-ray2.90A/B/C/D39-382[»]
6U2GX-ray2.89A2-393[»]
SMRiQ02750
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111590, 122 interactors
CORUMiQ02750
DIPiDIP-201N
ELMiQ02750
IntActiQ02750, 76 interactors
MINTiQ02750
STRINGi9606.ENSP00000302486

Chemistry databases

BindingDBiQ02750
ChEMBLiCHEMBL3587
DrugBankiDB06892 (5S)-4,5-difluoro-6-[(2-fluoro-4-iodophenyl)imino]-N-(2-hydroxyethoxy)cyclohexa-1,3-diene-1-carboxamide
DB07046 2-[(2-chloro-4-iodophenyl)amino]-N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluorobenzamide
DB08208 2-[(4-ETHYNYL-2-FLUOROPHENYL)AMINO]-3,4-DIFLUORO-N-(2-HYDROXYETHOXY)BENZAMIDE
DB03115 5-Bromo-N-(2,3-Dihydroxypropoxy)-3,4-Difluoro-2-[(2-Fluoro-4-Iodophenyl)Amino]Benzamide
DB06616 Bosutinib
DB05239 Cobimetinib
DB02152 K-252a
DB08130 N-(5-{3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]phenyl}-1,3,4-oxadiazol-2-yl)ethane-1,2-diamine
DB07101 PD-0325901
DB08911 Trametinib
DrugCentraliQ02750
GuidetoPHARMACOLOGYi2062

PTM databases

CarbonylDBiQ02750
iPTMnetiQ02750
PhosphoSitePlusiQ02750
SwissPalmiQ02750

Polymorphism and mutation databases

BioMutaiMAP2K1
DMDMi400274

Proteomic databases

CPTACiCPTAC-808
CPTAC-809
EPDiQ02750
jPOSTiQ02750
MassIVEiQ02750
MaxQBiQ02750
PaxDbiQ02750
PeptideAtlasiQ02750
PRIDEiQ02750
ProteomicsDBi58119 [Q02750-1]
58120 [Q02750-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5604

Genome annotation databases

EnsembliENST00000307102; ENSP00000302486; ENSG00000169032 [Q02750-1]
GeneIDi5604
KEGGihsa:5604
UCSCiuc010bhq.4 human [Q02750-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5604
DisGeNETi5604

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MAP2K1
GeneReviewsiMAP2K1
HGNCiHGNC:6840 MAP2K1
HPAiCAB003834
HPA026430
MalaCardsiMAP2K1
MIMi176872 gene
615279 phenotype
neXtProtiNX_Q02750
OpenTargetsiENSG00000169032
Orphaneti1340 Cardiofaciocutaneous syndrome
PharmGKBiPA30584

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0581 Eukaryota
ENOG410XQ5A LUCA
GeneTreeiENSGT00940000153487
HOGENOMiHOG000234206
InParanoidiQ02750
KOiK04368
OMAiGSEFQDF
OrthoDBi688282at2759
PhylomeDBiQ02750
TreeFamiTF105137

Enzyme and pathway databases

BRENDAi2.7.12.2 2681
ReactomeiR-HSA-110056 MAPK3 (ERK1) 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-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
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
SignaLinkiQ02750
SIGNORiQ02750

Miscellaneous databases

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

More...
ChiTaRSi
MAP2K1 human
EvolutionaryTraceiQ02750

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MAP2K1

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

More...
GenomeRNAii
5604
PharosiQ02750
PMAP-CutDBiQ02750

Protein Ontology

More...
PROi
PR:Q02750

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000169032 Expressed in 235 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ02750 baseline and differential
GenevisibleiQ02750 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 nameiMP2K1_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: Q02750
<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: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 215 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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