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UniProtKB - P14585 (LIN12_CAEEL)

Entry version 198 (29 Sep 2021)
Sequence version 1 (01 Jan 1990)
Previous versions | rss
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Protein

Protein lin-12

Gene

lin-12

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

Essential signaling protein which has a major role in many developmental processes; involved in cell fate decisions that require cell-cell interactions (PubMed:3419531, PubMed:3000611).

Probable membrane-bound receptor for putative ligands lag-2, apx-1, dsl-1 and osm-11 (PubMed:18036582, PubMed:18700817, PubMed:32053105, PubMed:3419531).

Upon ligand activation, and releasing from the cell membrane, the lin-12/Notch intracellular domain (NICD) forms a transcriptional activator complex with lag-1 and lag-3 and regulates expression of various genes (PubMed:8343960, PubMed:7566091, PubMed:16197940, PubMed:10830967, PubMed:16530045, PubMed:18381292).

Required for ventral cell fates in the postembryonic mesodermal lineage (M lineage) and in uterine precursor cells (PubMed:3419531, PubMed:18036582).

Activity in cell fate decisions and tumorigenesis is negatively regulated by sel-10 (PubMed:9389650).

Best known for involvement in cell-fate decisions during development, but also plays roles in other events (PubMed:10903169, PubMed:18599512, PubMed:21549604, PubMed:27661254).

Regulates recovery from the dauer larval state (PubMed:18599512).

Modulates chemosensory avoidance of octanol and quiescence during molting (PubMed:21549604).

Promotes basement membrane mobility during tissue remodeling (PubMed:27661254).

Involved in establishing left-right asymmetry during intestinal organogenesis (PubMed:10903169).

1 Publication16 Publications

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionActivator, Developmental protein
Biological processDifferentiation, Notch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

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

More...SignaLinki		P14585

<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:
Protein lin-12
Alternative name(s):
Abnormal cell lineage protein 12
Notch-like protein lin-121 Publication
Cleaved into the following chain:
lin-12/Notch intracellular domain2 Publications
<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:lin-12Imported
ORF Names:R107.8Imported
<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 lineageiEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditina › Rhabditomorpha › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis
<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 III

Organism-specific databases

WormBase

More...WormBasei		R107.8 ; CE00274 ; WBGene00003001 ; lin-12

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini16 – 908ExtracellularSequence analysisAdd BLAST893
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei909 – 931HelicalSequence analysisAdd BLAST23
Topological domaini932 – 1429CytoplasmicSequence analysisAdd BLAST498

Keywords - Cellular componenti

Cell membrane, 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 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

RNAi-mediated knockdown in cells of the pi uterine cell lineage results in impaired basement membrane mobility (PubMed:27661254). Knockdown on a glp-1 mutant background impairs octanol response when animals are shifted to the restrictive temperature (PubMed:21549604).2 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>Mutagenesisi400 – 1429Missing in n941; Increased total quiescence versus control animals. Affects cell fates of ventral, but not dorsal, postembryonic mesodermal lineage (M lineage). Similar, but enhanced phenotype seen when combined with RNAi-mediated knockdown of lag-2. On a sma-9 mutant background, reverses the dorsoventral polarity of the M lineage. Normal octanol response, but dramatically impaired when combined with RNAi-mediated knockdown of glp-1/Notch receptor. 2 PublicationsAdd BLAST1030

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 15Sequence analysisAdd BLAST15
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000763416 – 1429Protein lin-12Add BLAST1414
ChainiPRO_0000453171? – 1429lin-12/Notch intracellular domain2 Publications

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi24 ↔ 35By similarity
Disulfide bondi29 ↔ 49By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi41N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi51 ↔ 60By similarity
Disulfide bondi118 ↔ 129By similarity
Disulfide bondi123 ↔ 138By similarity
Disulfide bondi140 ↔ 149By similarity
Disulfide bondi156 ↔ 169By similarity
Disulfide bondi163 ↔ 178By similarity
Glycosylationi165N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi180 ↔ 189By similarity
Glycosylationi194N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi205 ↔ 227By similarity
Disulfide bondi221 ↔ 234By similarity
Disulfide bondi236 ↔ 245By similarity
Disulfide bondi254 ↔ 264By similarity
Disulfide bondi259 ↔ 273By similarity
Disulfide bondi275 ↔ 284By similarity
Disulfide bondi291 ↔ 302By similarity
Disulfide bondi296 ↔ 311By similarity
Disulfide bondi313 ↔ 322By similarity
Disulfide bondi327 ↔ 339By similarity
Disulfide bondi334 ↔ 351By similarity
Disulfide bondi353 ↔ 362By similarity
Disulfide bondi369 ↔ 381By similarity
Disulfide bondi375 ↔ 390By similarity
Glycosylationi378N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi392 ↔ 401By similarity
Disulfide bondi408 ↔ 419By similarity
Disulfide bondi413 ↔ 429By similarity
Disulfide bondi431 ↔ 440By similarity
Disulfide bondi462 ↔ 475By similarity
Disulfide bondi469 ↔ 480By similarity
Disulfide bondi482 ↔ 491By similarity
Disulfide bondi507 ↔ 518By similarity
Disulfide bondi512 ↔ 529By similarity
Glycosylationi515N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi531 ↔ 540By similarity
Disulfide bondi547 ↔ 558By similarity
Disulfide bondi552 ↔ 567By similarity
Disulfide bondi569 ↔ 578By similarity
Disulfide bondi586 ↔ 597By similarity
Disulfide bondi591 ↔ 607By similarity
Disulfide bondi609 ↔ 618By similarity
Glycosylationi623N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi638 ↔ 661By similarity
Disulfide bondi643 ↔ 656By similarity
Disulfide bondi652 ↔ 668By similarity
Disulfide bondi678 ↔ 702By similarity
Disulfide bondi684 ↔ 697By similarity
Disulfide bondi693 ↔ 709By similarity
Disulfide bondi716 ↔ 742By similarity
Disulfide bondi724 ↔ 737By similarity
Disulfide bondi733 ↔ 749By similarity
Glycosylationi751N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi754N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi900N-linked (GlcNAc...) asparagineSequence analysis1

<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

Upon binding its ligands, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain (By similarity). S2 cleavage is probably mediated by the metalloproteases adm-4 and sup-17 (PubMed:16197940). It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it from the cell membrane; S3 cleavage requires a multiprotein gamma-secretase complex, which may include presenilin sel-12 (PubMed:7566091).By similarity2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...PaxDbi		P14585

PRoteomics IDEntifications database

More...PRIDEi		P14585

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P14585

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in the postembryonic mesodermal lineage (M lineage) at the 4-M to 8-M stages, at similar levels in both the dorsal and the ventral sides (PubMed:18036582). At the 10-M stage and later, expression becomes more restricted along the anterioposterior axis and gradually lost in the anterior M lineage cells, but retained in the posterior M lineage cells (PubMed:18036582).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		WBGene00003001, Expressed in material anatomical entity and 4 other tissues

<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

May interact with dsl-1 (PubMed:18700817). May interact with lag-2 (PubMed:18700817). May interact with osm-11 (PubMed:18700817).

Interacts with sel-10 (PubMed:9389650).

2 Publications

When activated, the lin-12/Notch intracellular domain (NICD) can become a component of a complex consisting of at least the NICD, lag-1 and sel-8/lag-3 (PubMed:16530045, PubMed:18381292). The NICD probably facilitates ordered assembly of the ternary complex via allosteric interactions of its RBP-j associated molecule (RAM) domain with lag-1 (PubMed:16530045, PubMed:18381292).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		41481, 28 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3152, CSL-Notch-Mastermind transcription factor complex

Database of interacting proteins

More...DIPi		DIP-25208N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P14585

Protein interaction database and analysis system

More...IntActi		P14585, 5 interactors

STRING: functional protein association networks

More...STRINGi		6239.R107.8

<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

11429
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P14585

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P14585

<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>Domaini20 – 61EGF-like 1PROSITE-ProRule annotationAdd BLAST42
Domaini114 – 150EGF-like 2PROSITE-ProRule annotationAdd BLAST37
Domaini152 – 190EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini201 – 246EGF-like 4PROSITE-ProRule annotationAdd BLAST46
Domaini250 – 285EGF-like 5PROSITE-ProRule annotationAdd BLAST36
Domaini287 – 323EGF-like 6PROSITE-ProRule annotationAdd BLAST37
Domaini323 – 363EGF-like 7PROSITE-ProRule annotationAdd BLAST41
Domaini365 – 402EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini404 – 441EGF-like 9PROSITE-ProRule annotationAdd BLAST38
Domaini449 – 492EGF-like 10PROSITE-ProRule annotationAdd BLAST44
Domaini503 – 541EGF-like 11PROSITE-ProRule annotationAdd BLAST39
Domaini543 – 579EGF-like 12PROSITE-ProRule annotationAdd BLAST37
Domaini582 – 619EGF-like 13PROSITE-ProRule annotationAdd BLAST38
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati638 – 674LNR 1Add BLAST37
Repeati678 – 709LNR 2Add BLAST32
Repeati716 – 754LNR 3Add BLAST39
Repeati1093 – 1122ANK 1Add BLAST30
Repeati1126 – 1158ANK 2Add BLAST33
Repeati1162 – 1194ANK 3Add BLAST33
Repeati1206 – 1236ANK 4Add BLAST31
Repeati1240 – 1269ANK 5Add BLAST30

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>Regioni933 – 952RAM domain2 PublicationsAdd BLAST20
Regioni1308 – 1374DisorderedSequence analysisAdd BLAST67

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1308 – 1322Polar residuesSequence analysisAdd BLAST15
Compositional biasi1340 – 1374Polar residuesSequence analysisAdd BLAST35

<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 NOTCH family.Curated

Keywords - Domaini

ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1217, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00980000198606

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_005264_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P14585

Identification of Orthologs from Complete Genome Data

More...OMAi		TCIDSPL

Database of Orthologous Groups

More...OrthoDBi		7525at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P14585

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.20, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50027

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR035993, Notch-like_dom_sf
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 1 hit
PF00008, EGF, 6 hits
PF07645, EGF_CA, 1 hit
PF12661, hEGF, 3 hits
PF06816, NOD, 1 hit
PF07684, NODP, 1 hit
PF00066, Notch, 3 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01452, LNOTCHREPEAT

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00248, ANK, 6 hits
SM00181, EGF, 13 hits
SM00179, EGF_CA, 9 hits
SM00004, NL, 3 hits
SM01338, NOD, 1 hit
SM01339, NODP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48403, SSF48403, 1 hit
SSF57184, SSF57184, 1 hit
SSF90193, SSF90193, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 3 hits
PS00010, ASX_HYDROXYL, 3 hits
PS00022, EGF_1, 12 hits
PS01186, EGF_2, 11 hits
PS50026, EGF_3, 13 hits
PS01187, EGF_CA, 2 hits
PS50258, LNR, 3 hits

<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>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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P14585-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRIPTICFLF LLISLSKSLH IGSCLGLICG RNGHCHAGPV NGTQTSYWCR 
        60         70         80         90        100
CDEGFGGEYC EQQCDVSKCG ADEKCVFDKD YRMETCVCKD CDINGNSLLK 
       110        120        130        140        150
PSCPSGYGGD DCKTQGWCYP SVCMNGGQCI GAGNRAKCAC PDGFKGERCE 
       160        170        180        190        200
LDVNECEENK NACGNRSTCM NTLGTYICVC PQGFLPPDCL KPGNTSTVEF 
       210        220        230        240        250
KQPVCFLEIS ADHPDGRSMY CQNGGFCDKA SSKCQCPPGY HGSTCELLEK 
       260        270        280        290        300
EDSCASNPCS HGVCISFSGG FQCICDDGYS GSYCQEGKDN CVNNKCEAGS 
       310        320        330        340        350
KCINGVNSYF CDCPPERTGP YCEKMDCSAI PDICNHGTCI DSPLSEKAFE 
       360        370        380        390        400
CQCEPGYEGI LCEQDKNECL SENMCLNNGT CVNLPGSFRC DCARGFGGKW 
       410        420        430        440        450
CDEPLNMCQD FHCENDGTCM HTSDHSPVCQ CKNGFIGKRC EKECPIGFGG 
       460        470        480        490        500
VRCDLRLEIG ICSRQGGKCF NGGKCLSGFC VCPPDFTGNQ CEVNRKNGKS 
       510        520        530        540        550
SLSENLCLSD PCMNNATCID VDAHIGYACI CKQGFEGDIC ERHKDLCLEN 
       560        570        580        590        600
PCSNGGVCHQ HRESFSCDCP PGFYGNGCEQ EKMFRCLKST CQNGGVCINE 
       610        620        630        640        650
EEKGRKCECS YGFSGARCEE KINLTGFTEK DSLLRSVCEK RKCSERANDG 
       660        670        680        690        700
NCDADCNYAA CKFDGGDCSG KREPFSKCRY GNMCADFFAN GVCNQACNNE 
       710        720        730        740        750
ECLYDGMDCL PAVVRCPVKI REHCASRFAN GICDPECNTN GCGFDGGDCD 
       760        770        780        790        800
NETNATIITN IRITVQMDPK EFQVTGGQSL MEISSALRVT VRIQRDEEGP 
       810        820        830        840        850
LVFQWNGESE MDRVKMNERQ LTEQHVLSTS ISRKIKRSAT NIGVVVYLEV 
       860        870        880        890        900
QENCDTGKCL YKDAQSVVDS ISARLAKKGI DSFGIPISEA LVAEPRKSGN 
       910        920        930        940        950
NTGFLSWNAL LLIGAGCLIV MVVLMLGALP GNRTRKRRMI NASVWMPPME 
       960        970        980        990       1000
NEEKNRKNHQ SITSSQHSLL EASYDGYIKR QRNELQHYSL YPNPQGYGNG 
      1010       1020       1030       1040       1050
NDFLGDFNHT NLQIPTEPEP ESPIKLHTEA AGSYAITEPI TRESVNIIDP 
      1060       1070       1080       1090       1100
RHNRTVLHWI ASNSSAEKSE DLIVHEAKEC IAAGADVNAM DCDENTPLML 
      1110       1120       1130       1140       1150
AVLARRRRLV AYLMKAGADP TIYNKSERSA LHQAAANRDF GMMVYMLNST 
      1160       1170       1180       1190       1200
KLKGDIEELD RNGMTALMIV AHNEGRDQVA SAKLLVEKGA KVDYDGAARK 
      1210       1220       1230       1240       1250
DSEKYKGRTA LHYAAQVSNM PIVKYLVGEK GSNKDKQDED GKTPIMLAAQ 
      1260       1270       1280       1290       1300
EGRIEVVMYL IQQGASVEAV DATDHTARQL AQANNHHNIV DIFDRCRPER 
      1310       1320       1330       1340       1350
EYSMDLHIQH THQPQPSRKV TRAPKKQTSR SKKESASNSR DSTHLTPPPS 
      1360       1370       1380       1390       1400
DGSTSTPSPQ HFMNTTHTTP TSLNYLSPEY QTEAGSSEAF QPQCGAFGNG 
      1410       1420 
EMWYTRASTS YTQMQNEPMT RYSEPAHYF
Length:1,429
Mass (Da):157,116
Last modified:January 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i255EDD7A62C025DB
GO

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
M12069 Genomic DNA Translation: AAA70191.1
BX284603 Genomic DNA Translation: CAA78474.1

Protein sequence database of the Protein Information Resource

More...PIRi		S06434

NCBI Reference Sequences

More...RefSeqi		NP_499007.1, NM_066606.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		R107.8.1; R107.8.1; WBGene00003001

Database of genes from NCBI RefSeq genomes

More...GeneIDi		176282

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cel:CELE_R107.8

UCSC genome browser

More...UCSCi		R107.8, c. elegans

<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
M12069 Genomic DNA Translation: AAA70191.1
BX284603 Genomic DNA Translation: CAA78474.1
PIRiS06434
RefSeqiNP_499007.1, NM_066606.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FO1X-ray3.12E933-1297[»]
3BRDX-ray2.21D937-951[»]
3BRFX-ray2.47D938-950[»]
SMRiP14585
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi41481, 28 interactors
ComplexPortaliCPX-3152, CSL-Notch-Mastermind transcription factor complex
DIPiDIP-25208N
ELMiP14585
IntActiP14585, 5 interactors
STRINGi6239.R107.8

PTM databases

iPTMnetiP14585

Proteomic databases

PaxDbiP14585
PRIDEiP14585

Genome annotation databases

EnsemblMetazoaiR107.8.1; R107.8.1; WBGene00003001
GeneIDi176282
KEGGicel:CELE_R107.8
UCSCiR107.8, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		176282
WormBaseiR107.8 ; CE00274 ; WBGene00003001 ; lin-12

Phylogenomic databases

eggNOGiKOG1217, Eukaryota
GeneTreeiENSGT00980000198606
HOGENOMiCLU_005264_0_0_1
InParanoidiP14585
OMAiTCIDSPL
OrthoDBi7525at2759
PhylomeDBiP14585

Enzyme and pathway databases

SignaLinkiP14585

Miscellaneous databases

EvolutionaryTraceiP14585

Protein Ontology

More...PROi		PR:P14585

Gene expression databases

BgeeiWBGene00003001, Expressed in material anatomical entity and 4 other tissues

Family and domain databases

Gene3Di1.25.40.20, 1 hit
IDEALiIID50027
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR035993, Notch-like_dom_sf
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom
PfamiView protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 1 hit
PF00008, EGF, 6 hits
PF07645, EGF_CA, 1 hit
PF12661, hEGF, 3 hits
PF06816, NOD, 1 hit
PF07684, NODP, 1 hit
PF00066, Notch, 3 hits
PRINTSiPR01452, LNOTCHREPEAT
SMARTiView protein in SMART
SM00248, ANK, 6 hits
SM00181, EGF, 13 hits
SM00179, EGF_CA, 9 hits
SM00004, NL, 3 hits
SM01338, NOD, 1 hit
SM01339, NODP, 1 hit
SUPFAMiSSF48403, SSF48403, 1 hit
SSF57184, SSF57184, 1 hit
SSF90193, SSF90193, 3 hits
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 3 hits
PS00010, ASX_HYDROXYL, 3 hits
PS00022, EGF_1, 12 hits
PS01186, EGF_2, 11 hits
PS50026, EGF_3, 13 hits
PS01187, EGF_CA, 2 hits
PS50258, LNR, 3 hits

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 nameiLIN12_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: P14585
<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: January 1, 1990
Last sequence update: January 1, 1990
Last modified: September 29, 2021
This is version 198 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation 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

3D-structure, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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