UniProtKB - Q9NPJ3 (ACO13_HUMAN)
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- BLAST>sp|Q9NPJ3|ACO13_HUMAN Acyl-coenzyme A thioesterase 13 OS=Homo sapiens OX=9606 GN=ACOT13 PE=1 SV=1 MTSMTQSLREVIKAMTKARNFERVLGKITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLT ATLVDNISTMALLCTERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDL TNKATGKLIAQGRHTKHLGN
- Align
Acyl-coenzyme A thioesterase 13
ACOT13
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<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.12"Crystal structure of human thioesterase superfamily member 2."
Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D., Gong W.
Biochem. Biophys. Res. Commun. 349:172-177(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT. - Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=4.9 µM for n-decanoyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
- KM=26 µM for n-octanoyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
- KM=5 µM for myristoyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
- KM=9 µM for palmitoyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
- KM=9 µM for oleoyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
- KM=10 µM for 3,4-dihydroxyphenylacetyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
- KM=40 µM for 3-hydroxyphenylacetyl-CoA1 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
- Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 50 | Substrate | 1 |
<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
- acyl-CoA hydrolase activity Source: UniProtKB <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
<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
- acyl-CoA metabolic process Source: Reactome
- protein homotetramerization Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<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 function | Hydrolase |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.2.20. 2681. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-77289. Mitochondrial Fatty Acid Beta-Oxidation. |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q9NPJ3. |
<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: Acyl-coenzyme A thioesterase 13 (EC:3.1.2.-)Short name: Acyl-CoA thioesterase 13 Alternative name(s): Thioesterase superfamily member 2 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:ACOT13 Synonyms:THEM2 ORF Names:HT012, PNAS-27 |
| <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 | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> 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 | 9606 [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 › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <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
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000112304.10. |
Human Gene Nomenclature Database More...HGNCi | HGNC:20999. ACOT13. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 615652. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NPJ3. |
<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
Cytosol
- cytosol 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
- cytosol By similarity
Cytoskeleton
- spindle 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
- spindle By similarity
Mitochondrion
- Mitochondrion 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
- Mitochondrion By similarity
Nucleus
- Nucleus 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
Note: During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin.By similarity- Nucleus 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
Cytoskeleton
- spindle Source: UniProtKB-SubCell
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Mitochondrion
- mitochondrion Source: UniProtKB-SubCell
Nucleus
Other locations
- cytoplasm Source: GO_Central
<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, Cytoskeleton, Mitochondrion, 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
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 50 | N → A: Reduced activity. 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 | |
| <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>Mutagenesisi | 56 | H → A: Decreases affinity for substrate. 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 | |
| <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>Mutagenesisi | 65 | D → A: Loss of activity. 2 Publications <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/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>Mutagenesisi | 65 | D → E or N: Reduced activity. 2 Publications <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/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>Mutagenesisi | 83 | S → A: Reduced activity. 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 55856. |
Open Targets More...OpenTargetsi | ENSG00000112304. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA165617655. |
Chemistry databases
Drug and drug target database More...DrugBanki | DB08688. undecan-2-one. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ACOT13. |
<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000156697 | 1 – 140 | Acyl-coenzyme A thioesterase 13Add BLAST | 140 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <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_0000424501 | 2 – 140 | Acyl-coenzyme A thioesterase 13, N-terminally processedAdd BLAST | 139 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1 | N-acetylmethionineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 27 | N6-acetyllysineBy 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 | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 37 | N6-acetyllysineBy 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 | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 43 | N6-acetyllysineBy 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 | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 108 | N6-acetyllysineBy 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 | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 127 | N6-acetyllysineBy 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 | 1 |
<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
AcetylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NPJ3. |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NPJ3. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NPJ3. |
PeptideAtlas More...PeptideAtlasi | Q9NPJ3. |
PRoteomics IDEntifications database More...PRIDEi | Q9NPJ3. |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q9NPJ3-1. [Q9NPJ3-1] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NPJ3. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NPJ3. |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000112304. |
CleanEx database of gene expression profiles More...CleanExi | HS_THEM2. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NPJ3. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA019881. |
<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 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.12"Crystal structure of human thioesterase superfamily member 2."
Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D., Gong W.
Biochem. Biophys. Res. Commun. 349:172-177(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT. - Ref.13"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
<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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| MYDGF | Q969H8 | 4 | EBI-1045357,EBI-718622 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 120958. 25 interactors. |
Protein interaction database and analysis system More...IntActi | Q9NPJ3. 8 interactors. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000230048. |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 3 – 15 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 18 – 20 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 21 – 25 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 29 – 34 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 37 – 43 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 46 – 48 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 53 – 55 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 57 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 75 – 77 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 82 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 99 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 111 – 122 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 123 – 125 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 128 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2F0X | X-ray | 2.30 | A/B/C/D/E/F/G/H | 1-140 | [»] | |
| 2H4U | X-ray | 2.20 | A/B/C/D | 19-140 | [»] | |
| 3F5O | X-ray | 1.70 | A/B/C/D/E/F/G/H | 1-140 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NPJ3. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NPJ3. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9NPJ3. |
<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
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3328. Eukaryota. COG2050. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00390000013934. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000170540. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NPJ3. |
KEGG Orthology (KO) More...KOi | K17362. |
Identification of Orthologs from Complete Genome Data More...OMAi | KMGTLHG. |
Database of Orthologous Groups More...OrthoDBi | EOG091G125K. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NPJ3. |
TreeFam database of animal gene trees More...TreeFami | TF315062. |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029069. HotDog_dom_sf. IPR003736. PAAI_dom. IPR006683. Thioestr_dom. |
Pfam protein domain database More...Pfami | View protein in Pfam PF03061. 4HBT. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54637. SSF54637. 1 hit. |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00369. unchar_dom_1. 1 hit. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<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 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to 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
MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN
60 70 80 90 100
AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI
110 120 130 140
VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN
The sequence of this isoform differs from the canonical sequence as follows:
1-26: MTSMTQSLREVIKAMTKARNFERVLG → MVR
10 20 30 40 50
MVRKITLVSA APGKVICEMK VEEEHTNAIG TLHGGLTATL VDNISTMALL
60 70 80 90 100
CTERGAPGVS VDMNITYMSP AKLGEDIVIT AHVLKQGKTL AFTSVDLTNK
110
ATGKLIAQGR HTKHLGN
Alternative sequence
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 | AF155649 mRNA. Translation: AAF67006.1. AF220186 mRNA. Translation: AAF67651.1. AF274952 mRNA. Translation: AAK07529.1. AK000508 mRNA. Translation: BAA91215.1. AK309738 mRNA. No translation available. AL031775 Genomic DNA. No translation available. BC000894 mRNA. Translation: AAH00894.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4558.1. [Q9NPJ3-1] CCDS54972.1. [Q9NPJ3-2] |
NCBI Reference Sequences More...RefSeqi | NP_001153566.1. NM_001160094.1. [Q9NPJ3-2] NP_060943.1. NM_018473.3. [Q9NPJ3-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.731605. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1] ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55856. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55856. |
UCSC genome browser More...UCSCi | uc003nek.4. human. [Q9NPJ3-1] |
<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 | Organisms | Length | Cluster ID | Cluster name | Size | |
|---|---|---|---|---|---|---|---|
| Q9NPJ3 | Q5R833 UPI0000E4C91E | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) Homo sapiens (Human) | 140 | UniRef100_Q9NPJ3 | Cluster: Acyl-coenzyme A thioesterase 13 | 3 |
<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 | AF155649 mRNA. Translation: AAF67006.1. AF220186 mRNA. Translation: AAF67651.1. AF274952 mRNA. Translation: AAK07529.1. AK000508 mRNA. Translation: BAA91215.1. AK309738 mRNA. No translation available. AL031775 Genomic DNA. No translation available. BC000894 mRNA. Translation: AAH00894.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4558.1. [Q9NPJ3-1] CCDS54972.1. [Q9NPJ3-2] |
NCBI Reference Sequences More...RefSeqi | NP_001153566.1. NM_001160094.1. [Q9NPJ3-2] NP_060943.1. NM_018473.3. [Q9NPJ3-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.731605. |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2F0X | X-ray | 2.30 | A/B/C/D/E/F/G/H | 1-140 | [»] | |
| 2H4U | X-ray | 2.20 | A/B/C/D | 19-140 | [»] | |
| 3F5O | X-ray | 1.70 | A/B/C/D/E/F/G/H | 1-140 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NPJ3. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NPJ3. | |||||
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 | 120958. 25 interactors. |
Protein interaction database and analysis system More...IntActi | Q9NPJ3. 8 interactors. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000230048. |
Chemistry databases
Drug and drug target database More...DrugBanki | DB08688. undecan-2-one. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NPJ3. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NPJ3. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ACOT13. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NPJ3. |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NPJ3. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NPJ3. |
PeptideAtlas More...PeptideAtlasi | Q9NPJ3. |
PRoteomics IDEntifications database More...PRIDEi | Q9NPJ3. |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q9NPJ3-1. [Q9NPJ3-1] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1] ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55856. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55856. |
UCSC genome browser More...UCSCi | uc003nek.4. human. [Q9NPJ3-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 55856. |
DisGeNET More...DisGeNETi | 55856. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000112304.10. |
GeneCards: human genes, protein and diseases More...GeneCardsi | ACOT13. |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0005627. |
Human Gene Nomenclature Database More...HGNCi | HGNC:20999. ACOT13. |
Human Protein Atlas More...HPAi | HPA019881. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 615652. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NPJ3. |
Open Targets More...OpenTargetsi | ENSG00000112304. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA165617655. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3328. Eukaryota. COG2050. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00390000013934. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000170540. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NPJ3. |
KEGG Orthology (KO) More...KOi | K17362. |
Identification of Orthologs from Complete Genome Data More...OMAi | KMGTLHG. |
Database of Orthologous Groups More...OrthoDBi | EOG091G125K. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NPJ3. |
TreeFam database of animal gene trees More...TreeFami | TF315062. |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.2.20. 2681. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-77289. Mitochondrial Fatty Acid Beta-Oxidation. |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q9NPJ3. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | ACOT13. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9NPJ3. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 55856. |
Protein Ontology More...PROi | PR:Q9NPJ3. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000112304. |
CleanEx database of gene expression profiles More...CleanExi | HS_THEM2. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NPJ3. HS. |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029069. HotDog_dom_sf. IPR003736. PAAI_dom. IPR006683. Thioestr_dom. |
Pfam protein domain database More...Pfami | View protein in Pfam PF03061. 4HBT. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54637. SSF54637. 1 hit. |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00369. unchar_dom_1. 1 hit. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | ACO13_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9NPJ3Primary (citable) accession number: Q9NPJ3 Secondary accession number(s): F5H2L4, O95549 | |
| <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: | September 19, 2002 |
| Last sequence update: | October 1, 2000 | |
| Last modified: | March 28, 2018 | |
| This is version 149 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 | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |