UniProtKB - Q5T1C6 (THEM4_HUMAN)
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- BLAST>sp|Q5T1C6|THEM4_HUMAN Acyl-coenzyme A thioesterase THEM4 OS=Homo sapiens OX=9606 GN=THEM4 PE=1 SV=1 MLRSCAARLRTLGALCLPPVGRRLPGSEPRPELRSFSSEEVILKDCSVPNPSWNKDLRLL FDQFMKKCEDGSWKRLPSYKRTPTEWIQDFKTHFLDPKLMKEEQMSQAQLFTRSFDDGLG FEYVMFYNDIEKRMVCLFQGGPYLEGPPGFIHGGAIATMIDATVGMCAMMAGGIVMTANL NINYKRPIPLCSVVMINSQLDKVEGRKFFVSCNVQSVDEKTLYSEATSLFIKLNPAKSLT
- Align
Acyl-coenzyme A thioesterase THEM4
THEM4
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"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17. - Ref.7"Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways."
Ono H., Sakoda H., Fujishiro M., Anai M., Kushiyama A., Fukushima Y., Katagiri H., Ogihara T., Oka Y., Kamata H., Horike N., Uchijima Y., Kurihara H., Asano T.
Am. J. Physiol. 293:C1576-C1585(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.9"The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family."
Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.
Biochemistry 48:5507-5509(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.10"Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis."
Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S., Bozulic L., Hemmings B.A.
Cell. Signal. 21:639-650(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-37. - Ref.11"The carboxy-terminal modulator protein (CTMP) regulates mitochondrial dynamics."
Parcellier A., Tintignac L.A., Zhuravleva E., Dummler B., Brazil D.P., Hynx D., Cron P., Schenk S., Olivieri V., Hemmings B.A.
PLoS ONE 4:E5471-E5471(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.12"Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<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.9"The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family."
Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.
Biochemistry 48:5507-5509(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.12"Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
<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=2.4 µM for myristoyl-CoA2 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
- Ref.9"The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family."
Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.
Biochemistry 48:5507-5509(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.12"Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
- KM=2.6 µM for palmitoyl-CoA2 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
- Ref.9"The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family."
Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.
Biochemistry 48:5507-5509(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.12"Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
- KM=5.2 µM for oleoyl-CoA2 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
- Ref.9"The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family."
Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.
Biochemistry 48:5507-5509(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.12"Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 161 | Proton donor/acceptor1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <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 | 183 | Substrate | 1 | |
| <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 | 185 | 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: Reactome
- myristoyl-CoA hydrolase activity Source: UniProtKB-EC
- palmitoyl-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
- fatty acid metabolic process 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
- negative regulation of protein kinase B signaling Source: Reactome
- protein kinase B signaling Source: UniProtKB <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
- regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB <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>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 |
| Biological process | Apoptosis, Fatty acid metabolism, Lipid metabolism |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1257604 PIP3 activates AKT signaling R-HSA-165158 Activation of AKT2 R-HSA-199418 Negative regulation of the PI3K/AKT network R-HSA-389357 CD28 dependent PI3K/Akt signaling R-HSA-5218920 VEGFR2 mediated vascular permeability R-HSA-77289 Mitochondrial Fatty Acid Beta-Oxidation |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q5T1C6 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000657 |
<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 THEM4 (EC:3.1.2.2)Short name: Acyl-CoA thioesterase THEM4 Alternative name(s): Carboxyl-terminal modulator protein Thioesterase superfamily member 4 |
| <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:THEM4 Synonyms:CTMP |
| <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 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 | 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:ENSG00000159445.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:17947 THEM4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606388 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q5T1C6 |
<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
Plasma membrane
- Cell membrane 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
- Ref.1"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17.
- ruffle membrane 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
- Ref.1"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17.
- Cell membrane 1 Publication
Mitochondrion
- Mitochondrion 3 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
- Ref.8"Heat shock protein 70-mediated sensitization of cells to apoptosis by carboxyl-terminal modulator protein."
Piao L., Li Y., Yang K.J., Park K.A., Byun H.S., Won M., Hong J., Kim J.L., Kweon G.R., Hur G.M., Seok J.H., Cho J.Y., Chun T., Hess D., Sack R., Maira S.M., Brazil D.P., Hemmings B.A., Park J.
BMC Cell Biol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-37 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 37-SER-SER-38, SUBCELLULAR LOCATION. - Ref.10"Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis."
Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S., Bozulic L., Hemmings B.A.
Cell. Signal. 21:639-650(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-37. - Ref.11"The carboxy-terminal modulator protein (CTMP) regulates mitochondrial dynamics."
Parcellier A., Tintignac L.A., Zhuravleva E., Dummler B., Brazil D.P., Hynx D., Cron P., Schenk S., Olivieri V., Hemmings B.A.
PLoS ONE 4:E5471-E5471(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Mitochondrion inner membrane ; Peripheral membrane protein 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
- Ref.10"Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis."
Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S., Bozulic L., Hemmings B.A.
Cell. Signal. 21:639-650(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-37.
- Mitochondrion intermembrane space 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
- Ref.8"Heat shock protein 70-mediated sensitization of cells to apoptosis by carboxyl-terminal modulator protein."
Piao L., Li Y., Yang K.J., Park K.A., Byun H.S., Won M., Hong J., Kim J.L., Kweon G.R., Hur G.M., Seok J.H., Cho J.Y., Chun T., Hess D., Sack R., Maira S.M., Brazil D.P., Hemmings B.A., Park J.
BMC Cell Biol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-37 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 37-SER-SER-38, SUBCELLULAR LOCATION. - Ref.10"Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis."
Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S., Bozulic L., Hemmings B.A.
Cell. Signal. 21:639-650(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-37.
- Mitochondrion 3 Publications
Other locations
- Cytoplasm 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
- Ref.8"Heat shock protein 70-mediated sensitization of cells to apoptosis by carboxyl-terminal modulator protein."
Piao L., Li Y., Yang K.J., Park K.A., Byun H.S., Won M., Hong J., Kim J.L., Kweon G.R., Hur G.M., Seok J.H., Cho J.Y., Chun T., Hess D., Sack R., Maira S.M., Brazil D.P., Hemmings B.A., Park J.
BMC Cell Biol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-37 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 37-SER-SER-38, SUBCELLULAR LOCATION.
Note: Released from the mitochondria into the cytosol in response to apoptotic stimuli.1 Publication- Cytoplasm 1 Publication
- Ref.10"Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis."
Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S., Bozulic L., Hemmings B.A.
Cell. Signal. 21:639-650(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-37.
<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
Cytosol
- cytosol 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
Mitochondrion
- mitochondrial inner membrane Source: UniProtKB-SubCell
- mitochondrial intermembrane space Source: UniProtKB-SubCell
- mitochondrial matrix Source: Reactome
- mitochondrion 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
Plasma Membrane
- plasma membrane Source: Reactome
- ruffle membrane Source: UniProtKB-SubCell
<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
Cell membrane, Cell projection, Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane<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 | 37 – 38 | SS → DD: Abolishes import into the mitochondria. 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
| 2 | |
| <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 | 37 | S → A: Abolishes cleavage of mitochondrial transit peptide. 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 | 152 | H → A or F: Strongly reduced enzyme 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 | 161 | D → E or N: Nearly abolishes enzyme activity. Strongly reduced affinity for myristoyl-CoA. 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 | 177 | T → A: Strongly reduced enzyme 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 | 183 | N → A: No effect on enzyme 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 | 206 | R → A: Reduces enzyme 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 | 207 | K → A: Slightly reduced enzyme 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 | 117145 |
Open Targets More...OpenTargetsi | ENSG00000159445 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142670813 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | THEM4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74744451 |
<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei | 1 – 36 | MitochondrionSequence analysisAdd BLAST | 36 | |
| <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_0000314179 | 37 – 240 | Acyl-coenzyme A thioesterase THEM4Add BLAST | 204 |
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 | 37 | Phosphoserine1 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’ 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 | 38 | Phosphoserine1 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’ 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 | 55 | N6-succinyllysineBy 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 | 66 | N6-succinyllysineBy 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 | 74 | 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 | 98 | N6-succinyllysineBy 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 | 207 | N6-succinyllysineBy 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 <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.1"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17. - Ref.8"Heat shock protein 70-mediated sensitization of cells to apoptosis by carboxyl-terminal modulator protein."
Piao L., Li Y., Yang K.J., Park K.A., Byun H.S., Won M., Hong J., Kim J.L., Kweon G.R., Hur G.M., Seok J.H., Cho J.Y., Chun T., Hess D., Sack R., Maira S.M., Brazil D.P., Hemmings B.A., Park J.
BMC Cell Biol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-37 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 37-SER-SER-38, SUBCELLULAR LOCATION.
<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
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q5T1C6 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q5T1C6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q5T1C6 |
PeptideAtlas More...PeptideAtlasi | Q5T1C6 |
PRoteomics IDEntifications database More...PRIDEi | Q5T1C6 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 64259 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q5T1C6 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q5T1C6 |
<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.1"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17. - Ref.6"Hypermethylation and transcriptional downregulation of the carboxyl-terminal modulator protein gene in glioblastomas."
Knobbe C.B., Reifenberger J., Blaschke B., Reifenberger G.
J. Natl. Cancer Inst. 96:483-486(2004) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000159445 |
CleanEx database of gene expression profiles More...CleanExi | HS_THEM4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q5T1C6 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q5T1C6 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA028161 |
<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.1"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT ARG-17. - Ref.12"Correlation of structure and function in the human hotdog-fold enzyme hTHEM4."
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D., Luo L., Herzberg O., Dunaway-Mariano D.
Biochemistry 51:6490-6492(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, MUTAGENESIS OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207. - Ref.13"Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development."
Zhuravleva E., Gut H., Hynx D., Marcellin D., Bleck C.K., Genoud C., Cron P., Keusch J.J., Dummler B., Esposti M.D., Hemmings B.A.
Mol. Cell. Biol. 32:2685-2697(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 37-240, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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 |
|---|---|---|---|---|
| AKT1 | P31749 | 4 | EBI-7684443,EBI-296087 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 125557, 19 interactors |
Database of interacting proteins More...DIPi | DIP-60764N |
Protein interaction database and analysis system More...IntActi | Q5T1C6, 6 interactors |
Molecular INTeraction database More...MINTi | Q5T1C6 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000357804 |
<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 | 55 – 67 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 68 – 70 | 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 | 71 – 76 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 84 – 93 | 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 | |
| <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 | 111 – 113 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 117 – 119 | 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 | 120 – 128 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 129 – 132 | 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 | 4 | |
| <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 | 133 – 140 | 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 | 8 | |
| <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 | 142 – 144 | 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 | 145 – 147 | 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 | 153 – 172 | 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 | 20 | |
| <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 | 175 – 184 | 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 | |
| <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 | 193 – 204 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 207 – 216 | 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 | |
| <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 | 222 – 232 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 235 – 237 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q5T1C6 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q5T1C6 |
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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 206 – 207 | Substrate binding | 2 |
<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
<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
Transit peptidePhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4781 Eukaryota ENOG4111ZF6 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000018826 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000220857 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054340 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q5T1C6 |
KEGG Orthology (KO) More...KOi | K16339 |
Identification of Orthologs from Complete Genome Data More...OMAi | RKFFVSC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0G1S |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q5T1C6 |
TreeFam database of animal gene trees More...TreeFami | TF332518 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029069 HotDog_dom_sf 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 |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<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.
10 20 30 40 50
MLRSCAARLR TLGALCLPPV GRRLPGSEPR PELRSFSSEE VILKDCSVPN
60 70 80 90 100
PSWNKDLRLL FDQFMKKCED GSWKRLPSYK RTPTEWIQDF KTHFLDPKLM
110 120 130 140 150
KEEQMSQAQL FTRSFDDGLG FEYVMFYNDI EKRMVCLFQG GPYLEGPPGF
160 170 180 190 200
IHGGAIATMI DATVGMCAMM AGGIVMTANL NINYKRPIPL CSVVMINSQL
210 220 230 240
DKVEGRKFFV SCNVQSVDEK TLYSEATSLF IKLNPAKSLT
Natural variant
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 | AJ313515 mRNA Translation: CAC86384.1 AK314852 mRNA Translation: BAG37369.1 AL450992 Genomic DNA No translation available. CH471121 Genomic DNA Translation: EAW53400.1 BC065277 mRNA Translation: AAH65277.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1006.1 |
NCBI Reference Sequences More...RefSeqi | NP_444283.2, NM_053055.4 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.164070 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000368814; ENSP00000357804; ENSG00000159445 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 117145 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:117145 |
UCSC genome browser More...UCSCi | uc001ezj.3 human |
<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
Polymorphism<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 | |
|---|---|---|---|---|---|
| Q5T1C6 | UPI0005D03BD3 | 176 | |||
| THEM4 isoform 1 | 240 | ||||
| THEM4 isoform 1 | 240 | ||||
| Thioesterase superfamily member 4 | 240 | ||||
| Thioesterase superfamily member 4 | 240 | ||||
| +4 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q5T1C6 | UPI0005D03BD3 | 176 | |||
| Thioesterase superfamily member 4 | 240 | ||||
| Thioesterase superfamily member 4 | 240 | ||||
| Thioesterase superfamily member 4 | 240 | ||||
| THEM4 isoform 1 | 240 | ||||
| +72 | |||||
<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 | AJ313515 mRNA Translation: CAC86384.1 AK314852 mRNA Translation: BAG37369.1 AL450992 Genomic DNA No translation available. CH471121 Genomic DNA Translation: EAW53400.1 BC065277 mRNA Translation: AAH65277.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1006.1 |
NCBI Reference Sequences More...RefSeqi | NP_444283.2, NM_053055.4 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.164070 |
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 |
| 4AE8 | X-ray | 1.59 | A/B/C/D | 37-240 | [»] | |
| 4GAH | X-ray | 2.30 | A/B | 40-240 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q5T1C6 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q5T1C6 | |||||
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 | 125557, 19 interactors |
Database of interacting proteins More...DIPi | DIP-60764N |
Protein interaction database and analysis system More...IntActi | Q5T1C6, 6 interactors |
Molecular INTeraction database More...MINTi | Q5T1C6 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000357804 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000657 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q5T1C6 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q5T1C6 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | THEM4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74744451 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q5T1C6 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q5T1C6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q5T1C6 |
PeptideAtlas More...PeptideAtlasi | Q5T1C6 |
PRoteomics IDEntifications database More...PRIDEi | Q5T1C6 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 64259 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000368814; ENSP00000357804; ENSG00000159445 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 117145 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:117145 |
UCSC genome browser More...UCSCi | uc001ezj.3 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 117145 |
DisGeNET More...DisGeNETi | 117145 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000159445.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | THEM4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:17947 THEM4 |
Human Protein Atlas More...HPAi | HPA028161 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606388 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q5T1C6 |
Open Targets More...OpenTargetsi | ENSG00000159445 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142670813 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4781 Eukaryota ENOG4111ZF6 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000018826 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000220857 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054340 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q5T1C6 |
KEGG Orthology (KO) More...KOi | K16339 |
Identification of Orthologs from Complete Genome Data More...OMAi | RKFFVSC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0G1S |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q5T1C6 |
TreeFam database of animal gene trees More...TreeFami | TF332518 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1257604 PIP3 activates AKT signaling R-HSA-165158 Activation of AKT2 R-HSA-199418 Negative regulation of the PI3K/AKT network R-HSA-389357 CD28 dependent PI3K/Akt signaling R-HSA-5218920 VEGFR2 mediated vascular permeability R-HSA-77289 Mitochondrial Fatty Acid Beta-Oxidation |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q5T1C6 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | THEM4 human |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 117145 |
Protein Ontology More...PROi | PR:Q5T1C6 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000159445 |
CleanEx database of gene expression profiles More...CleanExi | HS_THEM4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q5T1C6 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q5T1C6 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029069 HotDog_dom_sf 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 |
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 | THEM4_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 | Q5T1C6Primary (citable) accession number: Q5T1C6 Secondary accession number(s): B2RBX2, Q96KR2 | |
| <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: | January 15, 2008 |
| Last sequence update: | December 21, 2004 | |
| Last modified: | July 18, 2018 | |
| This is version 123 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. | |
<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
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
