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Entry version 163 (18 Sep 2019)
Sequence version 4 (05 Jul 2004)
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Protein

Mitogen-activated protein kinase kinase kinase dlk-1

Gene

dlk-1

Organism
Caenorhabditis elegans
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

Component of a MAP kinase pathway that functions presynaptically to regulate synaptic architecture and presynaptic differentiation (PubMed:15707898). Phosphorylates and activates mkk-4 (PubMed:15707898). Has a role in axonal regrowth following injury and synaptogenesis (PubMed:19737525, PubMed:19164707). Also promotes tubulin post-translational modifications that protect microtubules (PubMed:23000142). Plays a role in cilium length regulation, possibly by reducing rab-5 mediated endocytosis, and may also have a role in intraflagellar transport in cilia (PubMed:26657059). Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord (PubMed:27123983).6 Publications
Isoform a: Has a role in synapse and axon development, and in axonal regrowth following injury.1 Publication
Isoform c: By forming heterooligomers with isoform a, acts as an inhibitor of isoform a activation. Its inhibitory function is independent of its catalytic activity.1 Publication

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

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

Mg2+By similarity

<p>This subsection of the <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

Isoform a: Inactive when associated with isoform c. Dissociation from isoform c, which is dependent on the phosphorylation of the C-terminal hexapeptide, results in self-association and activation. Transient increase in Ca2+ levels caused by axonal injury or synaptic activity triggers the dissociation of isoform a from isoform c; the dissociation may be influenced by the phosphorylation status of the C-terminal hexapeptide.1 Publication

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 sitei162ATPPROSITE-ProRule annotationBy similarity1
<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 sitei246Proton acceptorPROSITE-ProRule annotationBy similarity1

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 bindingi141 – 149ATPPROSITE-ProRule annotationBy similarity9

<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
Biological processNeurogenesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

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

More...
SignaLinki
O01700

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase dlk-1By similarity (EC:2.7.11.25By similarity)
Alternative name(s):
DAP kinase-like kinase
Death-associated protein kinase-like kinase
<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:dlk-1
ORF Names:F33E2.2
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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 I

Organism-specific databases

WormBase

More...
WormBasei
F33E2.2a ; CE36153 ; WBGene00001008 ; dlk-1
F33E2.2b ; CE36154 ; WBGene00001008 ; dlk-1
F33E2.2c ; CE36155 ; WBGene00001008 ; dlk-1
F33E2.2d ; CE23702 ; WBGene00001008 ; dlk-1

<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

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Overcome the lack of synaptogenesis caused by the loss of rpm-1 ubiquitin ligase activity (PubMed:17698012). Defects in axonal microtubule development (PubMed:19164707, PubMed:23000142). Double knockout with dlk-1 also suppresses the eva-1 receptor expression defect in the madd-3 single knockout (PubMed:27123983). Triple knockout with madd-3 and unc-54 results in paralysis (as in the unc-54 single knockout), and suppresses the lethality phenotype in the double madd-3 and unc-54 mutant (PubMed:27123983).4 Publications

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>Mutagenesisi312 – 928Missing in ju588; restores motor neuron normal presynapse morphology and number in a rpm-1 mutant background. 1 PublicationAdd BLAST617
Mutagenesisi363R → H in ju586; restores motor neuron normal presynapse morphology and number in a rpm-1 mutant background. 1 Publication1
Mutagenesisi449 – 480Missing : Prevents self-association or interaction with isoform c. 1 PublicationAdd BLAST32
Mutagenesisi459L → F in ju591; restores normal motor neuron presynapse morphology and number in a rpm-1 mutant background. 1 Publication1
Mutagenesisi523 – 928Missing in ju598; restores normal motor neuron presynaspe morphology and number in a rpm-1 mutant background. 1 PublicationAdd BLAST406
Mutagenesisi605 – 814Missing : Prevents interaction with isoform c. 1 PublicationAdd BLAST210
Mutagenesisi631 – 928Missing in ju476; does not affect c mRNA levels. Restores normal motor neuron presynapse morphology and number in a rpm-1 mutant background. 1 PublicationAdd BLAST298
Mutagenesisi816 – 928Missing in ju636; restores normal motor neuron presynapse morphology and number in a rpm-1 mutant background. 1 PublicationAdd BLAST113
Mutagenesisi870G → E in ju620; restores normal motor neuron presynapse morphology and number in a rpm-1 mutant background. 1 Publication1
Mutagenesisi874 – 879Missing : Abolishes self-association and enhances interaction with isoform c. 1 Publication6
Mutagenesisi874S → A: Prevents phosphorylation. Enhances binding to isoform c; when associated with A-878. 1 Publication1
Mutagenesisi874S → E: Phosphomimetic mutant. Enhances self-association and increases binding of the hexapeptide motif to the kinase domain; when associated with E-878. 1 Publication1
Mutagenesisi878S → A: Prevents phosphorylation. Enhances binding to isoform c; when associated with A-874. 1 Publication1
Mutagenesisi878S → E: Phosphomimetic mutant. Enhances self-association and increases binding of the hexapeptide motif to the kinase domain; when associated with E-874. 1 Publication1

<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_00003531981 – 928Mitogen-activated protein kinase kinase kinase dlk-1Add BLAST928

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 residuei874Phosphoserine1 Publication1
Modified residuei878Phosphoserine1 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

Ubiquitinated by rpm-1. Negatively regulated by ubiquitination by fsn-1 bound rpm-1, followed by degradation.1 Publication
Isoform a: Phosphorylation at Ser-874 and/or at Ser-878 abolishes interaction with isoform c and promotes binding to isoform a kinase domain (likely in trans) resulting in isoform a self-association and activation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
O01700

PRoteomics IDEntifications database

More...
PRIDEi
O01700

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O01700

<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

Expressed in nerve ring, nerve cord, neurons, and pharynx.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00001008 Expressed in 5 organ(s), highest expression level in multi-cellular organism

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O01700 baseline and differential

<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

Homooligomer (via leucine zipper domain and hexapeptide motif) (PubMed:23141066). Isoform a (via leucine zipper domain) forms a heterooligomer with isoform c (via leucine zipper domain) (PubMed:23141066). Isoform c does not self-associate (PubMed:23141066).

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-26475N

Protein interaction database and analysis system

More...
IntActi
O01700, 4 interactors

STRING: functional protein association networks

More...
STRINGi
6239.F33E2.2a

<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

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

More...
SMRi
O01700

Database of comparative protein structure models

More...
ModBasei
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>Domaini135 – 377Protein kinasePROSITE-ProRule annotationAdd BLAST243

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>Regioni459 – 480Leucine-zipper1 PublicationAdd BLAST22
Regioni605 – 814Important for interaction between isoform a and isoform c1 PublicationAdd BLAST210

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>Motifi874 – 879SDGLSD hexapeptide1 Publication6

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 biasi530 – 552Ser-richSequence analysisAdd BLAST23

<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

Isoform a: The C-terminal hexapeptide motif is required for homooligomerization and for its activation.1 Publication
Isoform a: The C-terminal domain is important for localization to synapses and axons.1 Publication

<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 kinase subfamily.By similarity

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4721 Eukaryota
ENOG410YKX2 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159006

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000112222

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O01700

KEGG Orthology (KO)

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KOi
K04422

Identification of Orthologs from Complete Genome Data

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OMAi
RETPYAN

Database of Orthologous Groups

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OrthoDBi
938929at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O01700

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR017419 MAP3K12_MAP3K13
IPR000719 Prot_kinase_dom
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF038165 MAPKKK12_MAPKKK13, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

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

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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 (4+)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 4 <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 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform aImported (identifier: O01700-1) [UniParc]FASTAAdd to basket
Also known as: DLK-1L1 Publication

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
MTSTTMVTTL DLVTPTSEEQ PGPAPESSDF STVVLSPDGS ELVTQSAPNT
60 70 80 90 100
PIQHREQANA EFGQKEGSPD PKNMVAATGN ASKPSLNSFY ADGLGQLRNG
110 120 130 140 150
LFSCFQPVFG YFGTKTTVEI EKSEDELWEI PFDAISELEW LGSGSQGAVF
160 170 180 190 200
RGQLENRTVA VKKVNQLKET EIKHLRHLRH QNIIEFLGVC SKSPCYCIVM
210 220 230 240 250
EYCSKGQLCT VLKSRNTITR ELFAQWVKEI ADGMHYLHQN KVIHRDLKSP
260 270 280 290 300
NILISAEDSI KICDFGTSHM QKKMDSTMMS FCGTVSWMAP EMIKKQPCNE
310 320 330 340 350
KVDVYSFGVV LWEMLTRETP YANIAQMAII FGVGTNILSL PMPEEAPKGL
360 370 380 390 400
VLLIKQCLSQ KGRNRPSFSH IRQHWEIFKP ELFEMTEEEW QLAWDSYREF
410 420 430 440 450
AKCIQYPSTV TRDHGGPKSA FAMEEEIQRK RHEQLNHIKD IRNMYEMKLK
460 470 480 490 500
RTNKMYDKLQ GCFTELKLKE SELAEWEKDL TEREQWHNQN SPKAVAAPRA
510 520 530 540 550
QLRGYPNEGY DDMSSDEDVQ PCRGSPYRCS NTSSSSGVQS SPFSRQSSSR
560 570 580 590 600
SSAGQQTRRS EGANPPKILR NDAIRHSGSY WETLGGARGS PARDSGFSQD
610 620 630 640 650
SGMWSAGAGS CTAINGGGQQ VCYSQTLYRN GDGRWSDGRI ASRRRVSTSV
660 670 680 690 700
NKSTAVPGQP VFFTRDSPSR VPHGVISCSS PRSSSKLNRS SYPSRNAPHQ
710 720 730 740 750
LEDGCCCAHA RAPRAKSIAV PMTSSSRARS PTPYDNDFEN AESFVDPESP
760 770 780 790 800
KNLKNLEKIV NLPESTSYDE ALCNSDVTMN PIYTSPITTY SNPCHVELVD
810 820 830 840 850
EENANDVDLT SSMDSRRSRS DDADVESSEE DEGNGNNILN TSMESEDLRY
860 870 880 890 900
RIDTSQSTMM SSLERSLEIG ATRSDGLSDN EMRVQAVKMS IKTHRRTGSN
910 920
PQALIHQCID EYTTSATDDS DDAGAVRI
Note: No experimental confirmation available.Curated
Length:928
Mass (Da):103,483
Last modified:July 5, 2004 - v4
<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:iEE071636ACAADBD4
GO
Isoform bImported (identifier: O01700-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     674-681: GVISCSSP → A

Note: No experimental confirmation available.Curated
Show »
Length:921
Mass (Da):102,824
Checksum:i302577E5324813B4
GO
Isoform cImported (identifier: O01700-3) [UniParc]FASTAAdd to basket
Also known as: DLK-1S1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     567-577: KILRNDAIRHS → SEYIFPEKLNI
     578-928: Missing.

Note: Produced by alternative polyadenylation. The alternative polyadenylation site is in intron 7. In neurons, the usage of this polyadenylation site is regulated by the antagonist action of sydn-1 and ssup-72.2 Publications
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Length:577
Mass (Da):65,401
Checksum:iBEDDDCCA10DB525A
GO
Isoform dImported (identifier: O01700-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

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Length:855
Mass (Da):95,787
Checksum:iF44DD2538CB7D95A
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
D6VPA3D6VPA3_CAEEL
Mitogen-activated protein kinase ki...
dlk-1 CELE_F33E2.2, F33E2.2
207Annotation score:

Annotation score:2 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>

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_0529641 – 73Missing in isoform d. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_052965567 – 577KILRNDAIRHS → SEYIFPEKLNI in isoform c. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_052966578 – 928Missing in isoform c. 1 PublicationAdd BLAST351
Alternative sequenceiVSP_052967674 – 681GVISCSSP → A in isoform b. 1 Publication8

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
BX284601, AL022593 Genomic DNA Translation: CAB06544.3
BX284601 Genomic DNA Translation: CAE54890.1
BX284601, AL022593 Genomic DNA Translation: CAE54891.1
BX284601, AL022593 Genomic DNA Translation: CAQ76474.1

Protein sequence database of the Protein Information Resource

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PIRi
B87950
T20082

NCBI Reference Sequences

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RefSeqi
NP_001021443.1, NM_001026272.3 [O01700-1]
NP_001021444.1, NM_001026273.5 [O01700-2]
NP_001021445.1, NM_001026274.3 [O01700-3]
NP_001129769.1, NM_001136297.2 [O01700-4]

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
F33E2.2a.1; F33E2.2a.1; WBGene00001008 [O01700-1]
F33E2.2b.1; F33E2.2b.1; WBGene00001008 [O01700-2]
F33E2.2c.1; F33E2.2c.1; WBGene00001008 [O01700-3]
F33E2.2d.1; F33E2.2d.1; WBGene00001008 [O01700-4]

Database of genes from NCBI RefSeq genomes

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GeneIDi
173128

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_F33E2.2

UCSC genome browser

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UCSCi
F33E2.2b c. elegans

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
BX284601, AL022593 Genomic DNA Translation: CAB06544.3
BX284601 Genomic DNA Translation: CAE54890.1
BX284601, AL022593 Genomic DNA Translation: CAE54891.1
BX284601, AL022593 Genomic DNA Translation: CAQ76474.1
PIRiB87950
T20082
RefSeqiNP_001021443.1, NM_001026272.3 [O01700-1]
NP_001021444.1, NM_001026273.5 [O01700-2]
NP_001021445.1, NM_001026274.3 [O01700-3]
NP_001129769.1, NM_001136297.2 [O01700-4]

3D structure databases

SMRiO01700
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-26475N
IntActiO01700, 4 interactors
STRINGi6239.F33E2.2a

PTM databases

iPTMnetiO01700

Proteomic databases

PaxDbiO01700
PRIDEiO01700

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF33E2.2a.1; F33E2.2a.1; WBGene00001008 [O01700-1]
F33E2.2b.1; F33E2.2b.1; WBGene00001008 [O01700-2]
F33E2.2c.1; F33E2.2c.1; WBGene00001008 [O01700-3]
F33E2.2d.1; F33E2.2d.1; WBGene00001008 [O01700-4]
GeneIDi173128
KEGGicel:CELE_F33E2.2
UCSCiF33E2.2b c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
173128
WormBaseiF33E2.2a ; CE36153 ; WBGene00001008 ; dlk-1
F33E2.2b ; CE36154 ; WBGene00001008 ; dlk-1
F33E2.2c ; CE36155 ; WBGene00001008 ; dlk-1
F33E2.2d ; CE23702 ; WBGene00001008 ; dlk-1

Phylogenomic databases

eggNOGiKOG4721 Eukaryota
ENOG410YKX2 LUCA
GeneTreeiENSGT00940000159006
HOGENOMiHOG000112222
InParanoidiO01700
KOiK04422
OMAiRETPYAN
OrthoDBi938929at2759
PhylomeDBiO01700

Enzyme and pathway databases

SignaLinkiO01700

Miscellaneous databases

Protein Ontology

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PROi
PR:O01700

Gene expression databases

BgeeiWBGene00001008 Expressed in 5 organ(s), highest expression level in multi-cellular organism
ExpressionAtlasiO01700 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR017419 MAP3K12_MAP3K13
IPR000719 Prot_kinase_dom
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PIRSFiPIRSF038165 MAPKKK12_MAPKKK13, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiDLK1_CAEEL
<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: O01700
Secondary accession number(s): B3KYB4, Q7JKE7, Q7JKE9
<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 4, 2008
Last sequence update: July 5, 2004
Last modified: September 18, 2019
This is version 163 of the entry and version 4 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 programCaenorhabditis annotation project

<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. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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