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Protein

Extracellular signal-regulated kinase 1

Gene

erkA

Organism
Dictyostelium discoideum (Slime mold)
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 transcript 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

Kinase involved in a signal transduction pathway.1 Publication

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

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

Mg2+By similarity

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

Activated by tyrosine and threonine phosphorylation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei178ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei275Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi155 – 163ATPPROSITE-ProRule annotation9

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

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: dictyBase

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
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.24 1939

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DDI-110056 MAPK3 (ERK1) activation
R-DDI-112409 RAF-independent MAPK1/3 activation
R-DDI-112411 MAPK1 (ERK2) activation
R-DDI-198753 ERK/MAPK targets
R-DDI-202670 ERKs are inactivated
R-DDI-2029482 Regulation of actin dynamics for phagocytic cup formation
R-DDI-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-DDI-3371453 Regulation of HSF1-mediated heat shock response
R-DDI-375165 NCAM signaling for neurite out-growth
R-DDI-442742 CREB phosphorylation through the activation of Ras
R-DDI-444257 RSK activation
R-DDI-445144 Signal transduction by L1
R-DDI-5663213 RHO GTPases Activate WASPs and WAVEs
R-DDI-5673001 RAF/MAP kinase cascade
R-DDI-5674135 MAP2K and MAPK activation
R-DDI-5674499 Negative feedback regulation of MAPK pathway
R-DDI-6798695 Neutrophil degranulation
R-DDI-881907 Gastrin-CREB signalling pathway via PKC and MAPK

<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:
Extracellular signal-regulated kinase 1 (EC:2.7.11.24)
Short name:
ERK1
Alternative name(s):
MAP kinase 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:erkA
Synonyms:erk1
ORF Names:DDB_G0286353
<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>OrganismiDictyostelium discoideum (Slime mold)
<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 identifieri44689 [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 lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
<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
  • UP000002195 <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> Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

Dictyostelium discoideum online informatics resource

More...
dictyBasei
DDB_G0286353 erkA

<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

GO - Cellular componenti

<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_00001863081 – 529Extracellular signal-regulated kinase 1Add BLAST529

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 residuei309PhosphothreonineBy similarity1
Modified residuei311PhosphotyrosineBy similarity1

<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

Dually phosphorylated on Thr-309 and Tyr-311, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P42525

PRoteomics IDEntifications database

More...
PRIDEi
P42525

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
44689.DDB0201635

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P42525

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

More...
SMRi
P42525

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini149 – 439Protein kinasePROSITE-ProRule annotationAdd BLAST291

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi309 – 311TXY3

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

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.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
KOG0660 Eukaryota
ENOG410XNY0 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P42525

KEGG Orthology (KO)

More...
KOi
K04371

Identification of Orthologs from Complete Genome Data

More...
OMAi
HTLFCLR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P42525

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008352 MAPK_p38-like
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01773 P38MAPKINASE

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01351 MAPK, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

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

<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.

P42525-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEPEFDHFQS QMDSDNTHQS TMFNVQDNNA ILMSGMENVL QSPRQLQAAA
60 70 80 90 100
QAQQQAAAQA QQQQVQAQQV QAQQAQQQQQ QQQNQQQQQQ QQNQQNQQQQ
110 120 130 140 150
QNQQQQSQQM TQQQLQQLMP PPPTSDTSNF NDNISYFVYG SQFTVPRRYS
160 170 180 190 200
IVKCIGHGAY GVVCSAKDNL TGEKVAIKKI SKAFDNLKDT KRTLREIHLL
210 220 230 240 250
RHFKHENLIS IKDILKPNSK EQFEDVYIVS ELMDTDLHQI ITSPQPLSDD
260 270 280 290 300
HCQYFVYQML RGLKHIHSAN VLHRDLKPSN LLINEDCLLK ICDLGLARVE
310 320 330 340 350
DATHQGFMTE YVATRWYRAP EVILSWNKYT KAIDIWSVGC IFAELLGRKP
360 370 380 390 400
LFQGKDYIHQ ITLIIETIGS PSEEDICNIA NEQARQFIRN MGNQPKVNFA
410 420 430 440 450
NMFPKANPDA IDLLERMLYF DPSKRLTVEE ALAHPYFQSL HDPSDEPICL
460 470 480 490 500
HKFSLNFEAW DLNRDLLKEL IYNEMLAYHP EDPQAPYYTD LNNPNFNLSR
510 520
IQSSSELFNL LQQQKQQIHQ QVNQQSIKN
Length:529
Mass (Da):61,303
Last modified:December 4, 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:i495C8ACD0215A3A7
GO

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

The sequence AAA59387 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti389R → RSL in AAA59387 (PubMed:15875012).Curated1
Sequence conflicti517Q → P in AAA59387 (PubMed:15875012).Curated1
Sequence conflicti529N → INN in AAA59387 (PubMed:15875012).Curated1

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
AAFI02000085 Genomic DNA Translation: EAL64201.1
U11077 mRNA Translation: AAA59387.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
A56042

NCBI Reference Sequences

More...
RefSeqi
XP_637704.1, XM_632612.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
EAL64201; EAL64201; DDB_G0286353

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8625569

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ddi:DDB_G0286353

<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
AAFI02000085 Genomic DNA Translation: EAL64201.1
U11077 mRNA Translation: AAA59387.1 Different initiation.
PIRiA56042
RefSeqiXP_637704.1, XM_632612.1

3D structure databases

ProteinModelPortaliP42525
SMRiP42525
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0201635

Proteomic databases

PaxDbiP42525
PRIDEiP42525

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL64201; EAL64201; DDB_G0286353
GeneIDi8625569
KEGGiddi:DDB_G0286353

Organism-specific databases

dictyBaseiDDB_G0286353 erkA

Phylogenomic databases

eggNOGiKOG0660 Eukaryota
ENOG410XNY0 LUCA
InParanoidiP42525
KOiK04371
OMAiHTLFCLR
PhylomeDBiP42525

Enzyme and pathway databases

BRENDAi2.7.11.24 1939
ReactomeiR-DDI-110056 MAPK3 (ERK1) activation
R-DDI-112409 RAF-independent MAPK1/3 activation
R-DDI-112411 MAPK1 (ERK2) activation
R-DDI-198753 ERK/MAPK targets
R-DDI-202670 ERKs are inactivated
R-DDI-2029482 Regulation of actin dynamics for phagocytic cup formation
R-DDI-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-DDI-3371453 Regulation of HSF1-mediated heat shock response
R-DDI-375165 NCAM signaling for neurite out-growth
R-DDI-442742 CREB phosphorylation through the activation of Ras
R-DDI-444257 RSK activation
R-DDI-445144 Signal transduction by L1
R-DDI-5663213 RHO GTPases Activate WASPs and WAVEs
R-DDI-5673001 RAF/MAP kinase cascade
R-DDI-5674135 MAP2K and MAPK activation
R-DDI-5674499 Negative feedback regulation of MAPK pathway
R-DDI-6798695 Neutrophil degranulation
R-DDI-881907 Gastrin-CREB signalling pathway via PKC and MAPK

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P42525

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008352 MAPK_p38-like
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PRINTSiPR01773 P38MAPKINASE
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERK1_DICDI
<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: P42525
Secondary accession number(s): Q54LX6
<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: November 1, 1995
Last sequence update: December 4, 2007
Last modified: December 5, 2018
This is version 132 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)

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
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