UniProtKB - Q09163 (DLK1_MOUSE)
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- BLAST>sp|Q09163|DLK1_MOUSE Protein delta homolog 1 OS=Mus musculus OX=10090 GN=Dlk1 PE=1 SV=1 MIATGALLRVLLLLLAFGHSTYGAECDPPCDPQYGFCEADNVCRCHVGWEGPLCDKCVTA PGCVNGVCKEPWQCICKDGWDGKFCEIDVRACTSTPCANNGTCVDLEKGQYECSCTPGFS GKDCQHKAGPCVINGSPCQHGGACVDDEGQASHASCLCPPGFSGNFCEIVAATNSCTPNP CENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCQNGGTCLQHTQVSFECLCKPP FMGPTCAKKRGASPVQVTHLPSGYGLTYRLTPGVHELPVQQPEQHILKVSMKELNKSTPL LTEGQAICFTILGVLTSLVVLGTVAIVFLNKCETWVSNLRYNHTFRKKKNLLLQYNSGEE LAVNIIFPEKIDMTTFNKEAGDEEI
- Align
Protein delta homolog 1
Dlk1
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"dlk, a putative mammalian homeotic gene differentially expressed in small cell lung carcinoma and neuroendocrine tumor cell line."
Laborda J., Sausville E.A., Hoffman T., Notario V.
J. Biol. Chem. 268:3817-3820(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. - Ref.2"Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation."
Smas C.M., Sul H.S.
Cell 73:725-734(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
<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
- calcium ion binding Source: InterPro
<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 - Biological processi
- bone mineralization Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cell differentiation Source: MGI
- embryonic skeletal system development Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- multicellular organism growth Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of bone remodeling Source: MGI
- negative regulation of fat cell differentiation Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of Notch signaling pathway Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- negative regulation of ossification Source: MGI
- negative regulation of osteoblast differentiation Source: MGI
- negative regulation of vascular endothelial cell proliferation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ossification Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- osteoblast differentiation Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of bone resorption Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of cytokine production Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- post-embryonic development Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of bone remodeling Source: MGI
- regulation of gene expression Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<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 delta homolog 1Short name: DLK-1 Alternative name(s): Adipocyte differentiation inhibitor protein Preadipocyte factor 1 Short name: Pref-1 Cleaved into the following chain: |
| <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:Dlk1 Synonyms:Dlk, Pref1, Scp-1 |
| <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>Organismi | Mus musculus (Mouse) |
| <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 identifieri | 10090 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
| <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 |
|
Organism-specific databases
Mouse genome database (MGD) from Mouse Genome Informatics (MGI) More...MGIi | MGI:94900 Dlk1 |
<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
Other locations
- Membrane ; Single-pass type I membrane protein
- Cytoplasm By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Extracellular region or secreted
- extracellular space Source: MGI
Plasma Membrane
- external side of plasma membrane Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: Reactome
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 domaini | 24 – 305 | ExtracellularSequence analysisAdd BLAST | 282 | |
| <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>Transmembranei | 306 – 329 | HelicalSequence analysisAdd BLAST | 24 | |
| <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 domaini | 330 – 385 | CytoplasmicSequence analysisAdd BLAST | 56 |
<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>Keywords - Cellular componenti
Cytoplasm, Membrane<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 peptidei | 1 – 23 | Sequence analysisAdd BLAST | 23 | |
| <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_0000007520 | 24 – 385 | Protein delta homolog 1Add BLAST | 362 | |
| <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_0000007521 | 24 – 305 | Fetal antigen 1Add BLAST | 282 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bondi | 26 ↔ 37 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 30 ↔ 43 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 45 ↔ 54 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 57 ↔ 68 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 63 ↔ 74 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 76 ↔ 85 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 92 ↔ 103 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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>GlycosylationiCAR_000160 | 94 | O-linked (GalNAc...) serine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 97 ↔ 113 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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>GlycosylationiCAR_000183 | 100 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 115 ↔ 124 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 131 ↔ 144 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 138 ↔ 156 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 158 ↔ 167 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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>Glycosylationi | 165 | N-linked (GlcNAc...) asparagine; atypical; partial1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 174 | N-linked (GlcNAc...) asparagine; atypical1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 176 ↔ 187 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 181 ↔ 196 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 198 ↔ 207 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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 bondi | 214 ↔ 225 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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>GlycosylationiCAR_000161 | 216 | O-linked (GalNAc...) serine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 219 ↔ 235 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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>GlycosylationiCAR_000162 | 224 | O-linked (GalNAc...) threonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 237 ↔ 246 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <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>Glycosylationi | 258 | O-linked (GalNAc...) threonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 267 | O-linked (GalNAc...) threonine; partial1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 271 | O-linked (GalNAc...) threonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 295 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA1) -- the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs."
Krogh T.N., Bachmann E., Teisner B., Skjoedt K., Hoejrup P.
Eur. J. Biochem. 244:334-342(1997) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT SER-94; ASN-100; ASN-165; ASN-174; SER-216; THR-224; THR-258; THR-267 AND THR-271, STRUCTURE OF CARBOHYDRATE.
<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>Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q09163 |
PRoteomics IDEntifications database More...PRIDEi | Q09163 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 153 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q09163 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q09163 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | Q09163 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"The novel gene EGFL9/Dlk2, highly homologous to Dlk1, functions as a modulator of adipogenesis."
Nueda M.L., Baladron V., Garcia-Ramirez J.J., Sanchez-Solana B., Ruvira M.D., Rivero S., Ballesteros M.A., Monsalve E.M., Diaz-Guerra M.J., Ruiz-Hidalgo M.J., Laborda J.
J. Mol. Biol. 367:1270-1280(2007) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"The novel gene EGFL9/Dlk2, highly homologous to Dlk1, functions as a modulator of adipogenesis."
Nueda M.L., Baladron V., Garcia-Ramirez J.J., Sanchez-Solana B., Ruvira M.D., Rivero S., Ballesteros M.A., Monsalve E.M., Diaz-Guerra M.J., Ruiz-Hidalgo M.J., Laborda J.
J. Mol. Biol. 367:1270-1280(2007) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Gene expression databases
CleanEx database of gene expression profiles More...CleanExi | MM_DLK1 |
<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
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 199231, 1 interactor |
Database of interacting proteins More...DIPi | DIP-6010N |
Protein interaction database and analysis system More...IntActi | Q09163, 1 interactor |
STRING: functional protein association networks More...STRINGi | 10090.ENSMUSP00000063104 |
<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 | Q09163 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q09163 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Domaini | 24 – 55 | EGF-like 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 32 | |
| <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>Domaini | 53 – 86 | EGF-like 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 34 | |
| <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>Domaini | 88 – 125 | EGF-like 3PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 38 | |
| <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>Domaini | 127 – 168 | EGF-like 4PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 42 | |
| <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>Domaini | 172 – 208 | EGF-like 5PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 37 | |
| <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>Domaini | 210 – 247 | EGF-like 6PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 38 |
<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>Keywords - Domaini
EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1217 Eukaryota ENOG410XP6K LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000072581 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG007065 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q09163 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q09163 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001881 EGF-like_Ca-bd_dom IPR013032 EGF-like_CS IPR000742 EGF-like_dom IPR000152 EGF-type_Asp/Asn_hydroxyl_site |
Pfam protein domain database More...Pfami | View protein in Pfam PF00008 EGF, 4 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00181 EGF, 6 hits SM00179 EGF_CA, 4 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00010 ASX_HYDROXYL, 1 hit PS00022 EGF_1, 5 hits PS01186 EGF_2, 6 hits PS50026 EGF_3, 6 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)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.
<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.
This entry describes 6 <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 basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE
60 70 80 90 100
GPLCDKCVTA PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN
110 120 130 140 150
GTCVDLEKGQ YECSCTPGFS GKDCQHKAGP CVINGSPCQH GGACVDDEGQ
160 170 180 190 200
ASHASCLCPP GFSGNFCEIV AATNSCTPNP CENDGVCTDI GGDFRCRCPA
210 220 230 240 250
GFVDKTCSRP VSNCASGPCQ NGGTCLQHTQ VSFECLCKPP FMGPTCAKKR
260 270 280 290 300
GASPVQVTHL PSGYGLTYRL TPGVHELPVQ QPEQHILKVS MKELNKSTPL
310 320 330 340 350
LTEGQAICFT ILGVLTSLVV LGTVAIVFLN KCETWVSNLR YNHTFRKKKN
360 370 380
LLLQYNSGEE LAVNIIFPEK IDMTTFNKEA GDEEI
The sequence of this isoform differs from the canonical sequence as follows:
231-281: Missing.
10 20 30 40 50
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE
60 70 80 90 100
GPLCDKCVTA PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN
110 120 130 140 150
GTCVDLEKGQ YECSCTPGFS GKDCQHKAGP CVINGSPCQH GGACVDDEGQ
160 170 180 190 200
ASHASCLCPP GFSGNFCEIV AATNSCTPNP CENDGVCTDI GGDFRCRCPA
210 220 230 240 250
GFVDKTCSRP VSNCASGPCQ NGGTCLQHTQ PEQHILKVSM KELNKSTPLL
260 270 280 290 300
TEGQAICFTI LGVLTSLVVL GTVAIVFLNK CETWVSNLRY NHTFRKKKNL
310 320 330
LLQYNSGEEL AVNIIFPEKI DMTTFNKEAG DEEI
The sequence of this isoform differs from the canonical sequence as follows:
231-303: Missing.
10 20 30 40 50
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE
60 70 80 90 100
GPLCDKCVTA PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN
110 120 130 140 150
GTCVDLEKGQ YECSCTPGFS GKDCQHKAGP CVINGSPCQH GGACVDDEGQ
160 170 180 190 200
ASHASCLCPP GFSGNFCEIV AATNSCTPNP CENDGVCTDI GGDFRCRCPA
210 220 230 240 250
GFVDKTCSRP VSNCASGPCQ NGGTCLQHTQ GQAICFTILG VLTSLVVLGT
260 270 280 290 300
VAIVFLNKCE TWVSNLRYNH TFRKKKNLLL QYNSGEELAV NIIFPEKIDM
310
TTFNKEAGDE EI
The sequence of this isoform differs from the canonical sequence as follows:
231-305: Missing.
10 20 30 40 50
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE
60 70 80 90 100
GPLCDKCVTA PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN
110 120 130 140 150
GTCVDLEKGQ YECSCTPGFS GKDCQHKAGP CVINGSPCQH GGACVDDEGQ
160 170 180 190 200
ASHASCLCPP GFSGNFCEIV AATNSCTPNP CENDGVCTDI GGDFRCRCPA
210 220 230 240 250
GFVDKTCSRP VSNCASGPCQ NGGTCLQHTQ AICFTILGVL TSLVVLGTVA
260 270 280 290 300
IVFLNKCETW VSNLRYNHTF RKKKNLLLQY NSGEELAVNI IFPEKIDMTT
310
FNKEAGDEEI
The sequence of this isoform differs from the canonical sequence as follows:
211-303: Missing.
10 20 30 40 50
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE
60 70 80 90 100
GPLCDKCVTA PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN
110 120 130 140 150
GTCVDLEKGQ YECSCTPGFS GKDCQHKAGP CVINGSPCQH GGACVDDEGQ
160 170 180 190 200
ASHASCLCPP GFSGNFCEIV AATNSCTPNP CENDGVCTDI GGDFRCRCPA
210 220 230 240 250
GFVDKTCSRP GQAICFTILG VLTSLVVLGT VAIVFLNKCE TWVSNLRYNH
260 270 280 290
TFRKKKNLLL QYNSGEELAV NIIFPEKIDM TTFNKEAGDE EI
The sequence of this isoform differs from the canonical sequence as follows:
211-305: Missing.
10 20 30 40 50
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE
60 70 80 90 100
GPLCDKCVTA PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN
110 120 130 140 150
GTCVDLEKGQ YECSCTPGFS GKDCQHKAGP CVINGSPCQH GGACVDDEGQ
160 170 180 190 200
ASHASCLCPP GFSGNFCEIV AATNSCTPNP CENDGVCTDI GGDFRCRCPA
210 220 230 240 250
GFVDKTCSRP AICFTILGVL TSLVVLGTVA IVFLNKCETW VSNLRYNHTF
260 270 280 290
RKKKNLLLQY NSGEELAVNI IFPEKIDMTT FNKEAGDEEI
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 250 | R → P in AAA37175 (PubMed:8500166).Curated | 1 | |
| <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 conflicti | 320 – 385 | VLGTV…GDEEI → CWAPWPSSFSTSAKPGCPTC ATTTCFARRRTSCCSITAAR SWRSISSSPRRLT in AAA37175 (PubMed:8500166).CuratedAdd BLAST | 66 | |
| <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 conflicti | 344 – 345 | TF → ML in BAA04121 (Ref. 4) Curated | 2 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti | 347 | Missing 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001379 | 211 – 305 | Missing in isoform D2. CuratedAdd BLAST | 95 | |
| <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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001378 | 211 – 303 | Missing in isoform D. CuratedAdd BLAST | 93 | |
| <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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001382 | 231 – 305 | Missing in isoform C2. CuratedAdd BLAST | 75 | |
| <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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001381 | 231 – 303 | Missing in isoform C. CuratedAdd BLAST | 73 | |
| <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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001380 | 231 – 281 | Missing in isoform B. CuratedAdd BLAST | 51 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | Z12171 mRNA Translation: CAA78162.1 U15980 mRNA Translation: AAB60495.1 L12721 mRNA Translation: AAA37175.1 S71340 Genomic DNA No translation available. D16847 mRNA Translation: BAA04121.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS26168.1 [Q09163-1] CCDS49173.1 [Q09163-6] CCDS49174.1 [Q09163-2] CCDS56863.1 [Q09163-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A54785 S53718 |
NCBI Reference Sequences More...RefSeqi | NP_034182.2, NM_010052.5 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Mm.157069 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 13386 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mmu:13386 |
<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>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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q09163 | Delta-like 1 (Fragment) | 65 | |||
| Delta-like 1 (Fragment) | 20 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q09163 | Delta-like 1 (Fragment) | 65 | |||
| Delta-like 1 (Fragment) | 20 | ||||
| UPI000A306DDF | 385 | ||||
| UPI000A31881F | 385 | ||||
| Protein delta homolog 1 | 383 | ||||
| +10 | |||||
| Q09163-2 | Dlk1 | 334 | |||
| UPI000A30D3BE | 334 | ||||
| UPI000A316EC3 | 334 | ||||
| UPI0000DBFBD9 | 332 | ||||
| UPI00077DB9C4 | 325 | ||||
| Q09163-3 | Dlk1 | 312 | |||
| UPI000A30917E | 312 | ||||
| UPI000A3189AC | 312 | ||||
| protein delta homolog 1 isoform X2 | 310 | ||||
| UPI00067DD3E2 | 308 | ||||
| +4 | |||||
| Q09163-4 | Dlk1 | 312 | |||
| UPI000A30917E | 312 | ||||
| UPI000A3189AC | 312 | ||||
| protein delta homolog 1 isoform X2 | 310 | ||||
| UPI00067DD3E2 | 308 | ||||
| +4 | |||||
| Q09163-5 | Protein delta homolog 1 | 292 | |||
| UPI000A31176D | 290 | ||||
| UPI000A3198C8 | 290 | ||||
| UPI00042AAB5F | 288 | ||||
| Protein delta homolog 1 | 290 | ||||
| +1 | |||||
| Q09163-6 | Protein delta homolog 1 | 292 | |||
| UPI000A31176D | 290 | ||||
| UPI000A3198C8 | 290 | ||||
| UPI00042AAB5F | 288 | ||||
| Q09163-5 | 292 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q09163 | Delta-like 1 (Fragment) | 65 | |||
| Delta-like 1 (Fragment) | 20 | ||||
| UPI000A31881F | 385 | ||||
| UPI000A306DDF | 385 | ||||
| protein delta homolog 1 isoform X1 | 383 | ||||
| +69 | |||||
| Q09163-5 | Protein delta homolog 1 | 292 | |||
| UPI000A31176D | 290 | ||||
| UPI000A3198C8 | 290 | ||||
| UPI00042AAB5F | 288 | ||||
| UPI0006D710CB | 309 | ||||
| +38 | |||||
| Q09163-6 | Protein delta homolog 1 | 292 | |||
| UPI000A31176D | 290 | ||||
| UPI000A3198C8 | 290 | ||||
| UPI00042AAB5F | 288 | ||||
| UPI0006D710CB | 309 | ||||
| +38 | |||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | Z12171 mRNA Translation: CAA78162.1 U15980 mRNA Translation: AAB60495.1 L12721 mRNA Translation: AAA37175.1 S71340 Genomic DNA No translation available. D16847 mRNA Translation: BAA04121.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS26168.1 [Q09163-1] CCDS49173.1 [Q09163-6] CCDS49174.1 [Q09163-2] CCDS56863.1 [Q09163-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A54785 S53718 |
NCBI Reference Sequences More...RefSeqi | NP_034182.2, NM_010052.5 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Mm.157069 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q09163 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q09163 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 199231, 1 interactor |
Database of interacting proteins More...DIPi | DIP-6010N |
Protein interaction database and analysis system More...IntActi | Q09163, 1 interactor |
STRING: functional protein association networks More...STRINGi | 10090.ENSMUSP00000063104 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 153 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q09163 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q09163 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | Q09163 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q09163 |
PRoteomics IDEntifications database More...PRIDEi | Q09163 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 13386 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mmu:13386 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 8788 |
Mouse genome database (MGD) from Mouse Genome Informatics (MGI) More...MGIi | MGI:94900 Dlk1 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1217 Eukaryota ENOG410XP6K LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000072581 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG007065 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q09163 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q09163 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | Dlk1 mouse |
Protein Ontology More...PROi | PR:Q09163 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
CleanEx database of gene expression profiles More...CleanExi | MM_DLK1 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001881 EGF-like_Ca-bd_dom IPR013032 EGF-like_CS IPR000742 EGF-like_dom IPR000152 EGF-type_Asp/Asn_hydroxyl_site |
Pfam protein domain database More...Pfami | View protein in Pfam PF00008 EGF, 4 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00181 EGF, 6 hits SM00179 EGF_CA, 4 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00010 ASX_HYDROXYL, 1 hit PS00022 EGF_1, 5 hits PS01186 EGF_2, 6 hits PS50026 EGF_3, 6 hits |
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 namei | DLK1_MOUSE | |
| <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>Accessioni | Q09163Primary (citable) accession number: Q09163 Secondary accession number(s): Q07645, Q62208 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
| Last sequence update: | November 1, 1995 | |
| Last modified: | July 18, 2018 | |
| This is version 158 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
<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
<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>Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
