UniProtKB - P06753 (TPM3_HUMAN)
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- BLAST>sp|P06753|TPM3_HUMAN Tropomyosin alpha-3 chain OS=Homo sapiens OX=9606 GN=TPM3 PE=1 SV=2 MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDK YSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA ADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERT EERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRA EFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
- Align
Tropomyosin alpha-3 chain
TPM3
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 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
Caution
<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
- actin filament binding Source: GO_Central
- structural constituent of muscle Source: GO_Central
<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
- actin filament organization Source: GO_Central
- muscle contraction Source: GO_Central
- muscle filament sliding Source: Reactome
<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 | Actin-binding, Muscle protein |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-390522 Striated Muscle Contraction R-HSA-445355 Smooth Muscle Contraction |
<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: Tropomyosin alpha-3 chainAlternative name(s): Gamma-tropomyosin Tropomyosin-3 Tropomyosin-5 Short name: hTM5 |
| <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:TPM3 |
| <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:ENSG00000143549.19 |
Human Gene Nomenclature Database More...HGNCi | HGNC:12012 TPM3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 164970 gene 191030 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P06753 |
<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
Cytoskeleton
- cytoskeleton Curated
Cytoskeleton
- actin cytoskeleton Source: HPA
- actin filament Source: GO_Central
- cytoskeleton Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- muscle thin filament tropomyosin Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- stress fiber Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
<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<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Nemaline myopathy 1 (NEM1)4 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.22"A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy."
Laing N.G., Wilton S.D., Akkari P.A., Dorosz S., Boundy K., Kneebone C., Blumbergs P., White S., Watkins H., Love D.R., Haan E.
Nat. Genet. 9:75-79(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NEM1 ARG-9. - Ref.23"A nemaline myopathy mutation in alpha-tropomyosin causes defective regulation of striated muscle force production."
Michele D.E., Albayya F.P., Metzger J.M.
J. Clin. Invest. 104:1575-1581(1999) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT NEM1 ARG-9. - Ref.24"A second pedigree with autosomal dominant nemaline myopathy caused by TPM3 mutation: a clinical and pathological study."
Penisson-Besnier I., Monnier N., Toutain A., Dubas F., Laing N.
Neuromuscul. Disord. 17:330-337(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NEM1 HIS-168. - Ref.30"Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies."
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C., Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M., Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M., Kang P.B., Klinge L., Kolski H. , Lochmueller H., Magy L., Manel V., Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H., Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M., Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N., Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.
Hum. Mutat. 35:779-790(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEM1 PHE-88 AND CYS-168, VARIANTS CAPM1 PHE-88; ALA-151; CYS-168 AND ILE-245, VARIANTS CFTD VAL-100; CYS-168 AND HIS-168, VARIANTS CYS-91 AND LYS-253.
Laing N.G., Wilton S.D., Akkari P.A., Dorosz S., Boundy K., Kneebone C., Blumbergs P., White S., Watkins H., Love D.R., Haan E.
Nat. Genet. 9:75-79(1995) [PubMed] [Europe PMC] [Abstract]
Michele D.E., Albayya F.P., Metzger J.M.
J. Clin. Invest. 104:1575-1581(1999) [PubMed] [Europe PMC] [Abstract]
Penisson-Besnier I., Monnier N., Toutain A., Dubas F., Laing N.
Neuromuscul. Disord. 17:330-337(2007) [PubMed] [Europe PMC] [Abstract]
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C., Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M., Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M., Kang P.B., Klinge L., Kolski H. , Lochmueller H., Magy L., Manel V., Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H., Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M., Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N., Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.
Hum. Mutat. 35:779-790(2014) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_013460 | 9 | M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070069 | 168 | R → H in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy. 6 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>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.11"A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences."
Martin-Zanca D., Hughes S.H., Barbacid M.
Nature 319:743-748(1986) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH NTRK1.
Myopathy, congenital, with fiber-type disproportion (CFTD)4 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.25"Mutations in TPM3 are a common cause of congenital fiber type disproportion."
Clarke N.F., Kolski H., Dye D.E., Lim E., Smith R.L., Patel R., Fahey M.C., Bellance R., Romero N.B., Johnson E.S., Labarre-Vila A., Monnier N., Laing N.G., North K.N.
Ann. Neurol. 63:329-337(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CFTD MET-100; CYS-168; GLY-168; GLU-169 AND GLY-245, VARIANT CAPM1 HIS-168. - Ref.28"Mutations of tropomyosin 3 (TPM3) are common and associated with type 1 myofiber hypotrophy in congenital fiber type disproportion."
Lawlor M.W., Dechene E.T., Roumm E., Geggel A.S., Moghadaszadeh B., Beggs A.H.
Hum. Mutat. 31:176-183(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CFTD VAL-4; PRO-91; HIS-168 AND LYS-241. - Ref.29"Congenital fibre type disproportion associated with mutations in the tropomyosin 3 (TPM3) gene mimicking congenital myasthenia."
Munot P., Lashley D., Jungbluth H., Feng L., Pitt M., Robb S.A., Palace J., Jayawant S., Kennet R., Beeson D., Cullup T., Abbs S., Laing N., Sewry C., Muntoni F.
Neuromuscul. Disord. 20:796-800(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CFTD HIS-168 AND ALA-174. - Ref.30"Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies."
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C., Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M., Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M., Kang P.B., Klinge L., Kolski H. , Lochmueller H., Magy L., Manel V., Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H., Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M., Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N., Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.
Hum. Mutat. 35:779-790(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEM1 PHE-88 AND CYS-168, VARIANTS CAPM1 PHE-88; ALA-151; CYS-168 AND ILE-245, VARIANTS CFTD VAL-100; CYS-168 AND HIS-168, VARIANTS CYS-91 AND LYS-253.
Clarke N.F., Kolski H., Dye D.E., Lim E., Smith R.L., Patel R., Fahey M.C., Bellance R., Romero N.B., Johnson E.S., Labarre-Vila A., Monnier N., Laing N.G., North K.N.
Ann. Neurol. 63:329-337(2008) [PubMed] [Europe PMC] [Abstract]
Lawlor M.W., Dechene E.T., Roumm E., Geggel A.S., Moghadaszadeh B., Beggs A.H.
Hum. Mutat. 31:176-183(2010) [PubMed] [Europe PMC] [Abstract]
Munot P., Lashley D., Jungbluth H., Feng L., Pitt M., Robb S.A., Palace J., Jayawant S., Kennet R., Beeson D., Cullup T., Abbs S., Laing N., Sewry C., Muntoni F.
Neuromuscul. Disord. 20:796-800(2010) [PubMed] [Europe PMC] [Abstract]
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C., Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M., Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M., Kang P.B., Klinge L., Kolski H. , Lochmueller H., Magy L., Manel V., Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H., Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M., Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N., Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.
Hum. Mutat. 35:779-790(2014) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071499 | 4 | A → V in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071502 | 91 | R → P in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070066 | 100 | L → M in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071503 | 100 | L → V in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070067 | 168 | R → C in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070068 | 168 | R → G in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070070 | 169 | K → E in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071506 | 174 | E → A in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071507 | 241 | E → K in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070071 | 245 | R → G in CFTD. 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 |
Cap myopathy 1 (CAPM1)5 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.25"Mutations in TPM3 are a common cause of congenital fiber type disproportion."
Clarke N.F., Kolski H., Dye D.E., Lim E., Smith R.L., Patel R., Fahey M.C., Bellance R., Romero N.B., Johnson E.S., Labarre-Vila A., Monnier N., Laing N.G., North K.N.
Ann. Neurol. 63:329-337(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CFTD MET-100; CYS-168; GLY-168; GLU-169 AND GLY-245, VARIANT CAPM1 HIS-168. - Ref.26"TPM3 mutation in one of the original cases of cap disease."
Ohlsson M., Fidzianska A., Tajsharghi H., Oldfors A.
Neurology 72:1961-1963(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CAPM1 CYS-168. - Ref.27"A TPM3 mutation causing cap myopathy."
De Paula A.M., Franques J., Fernandez C., Monnier N., Lunardi J., Pellissier J.F., Figarella-Branger D., Pouget J.
Neuromuscul. Disord. 19:685-688(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CAPM1 HIS-168. - Ref.30"Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies."
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C., Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M., Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M., Kang P.B., Klinge L., Kolski H. , Lochmueller H., Magy L., Manel V., Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H., Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M., Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N., Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.
Hum. Mutat. 35:779-790(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEM1 PHE-88 AND CYS-168, VARIANTS CAPM1 PHE-88; ALA-151; CYS-168 AND ILE-245, VARIANTS CFTD VAL-100; CYS-168 AND HIS-168, VARIANTS CYS-91 AND LYS-253. - Ref.31"Novel TPM3 mutation in a family with cap myopathy and review of the literature."
Schreckenbach T., Schroeder J.M., Voit T., Abicht A., Neuen-Jacob E., Roos A., Bulst S., Kuhl C., Schulz J.B., Weis J., Claeys K.G.
Neuromuscul. Disord. 24:117-124(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CAPM1 ILE-149.
Clarke N.F., Kolski H., Dye D.E., Lim E., Smith R.L., Patel R., Fahey M.C., Bellance R., Romero N.B., Johnson E.S., Labarre-Vila A., Monnier N., Laing N.G., North K.N.
Ann. Neurol. 63:329-337(2008) [PubMed] [Europe PMC] [Abstract]
Ohlsson M., Fidzianska A., Tajsharghi H., Oldfors A.
Neurology 72:1961-1963(2009) [PubMed] [Europe PMC] [Abstract]
De Paula A.M., Franques J., Fernandez C., Monnier N., Lunardi J., Pellissier J.F., Figarella-Branger D., Pouget J.
Neuromuscul. Disord. 19:685-688(2009) [PubMed] [Europe PMC] [Abstract]
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C., Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M., Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M., Kang P.B., Klinge L., Kolski H. , Lochmueller H., Magy L., Manel V., Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H., Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M., Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N., Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.
Hum. Mutat. 35:779-790(2014) [PubMed] [Europe PMC] [Abstract]
Schreckenbach T., Schroeder J.M., Voit T., Abicht A., Neuen-Jacob E., Roos A., Bulst S., Kuhl C., Schulz J.B., Weis J., Claeys K.G.
Neuromuscul. Disord. 24:117-124(2014) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071504 | 149 | L → I in CAPM1. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071505 | 151 | E → A in CAPM1. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071508 | 245 | R → I in CAPM1. 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>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 - Diseasei
Disease mutation, Nemaline myopathy, Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 7170 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | TPM3 |
MalaCards human disease database More...MalaCardsi | TPM3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 255310 phenotype 609284 phenotype |
Open Targets More...OpenTargetsi | ENSG00000143549 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 171881 Cap myopathy 171439 Childhood-onset nemaline myopathy 2020 Congenital fiber-type disproportion myopathy 178342 Inflammatory myofibroblastic tumor 171433 Intermediate nemaline myopathy |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36692 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 519668659 |
<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / 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 | RemovedBy 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 | ||||
| <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_0000205632 | 2 – 285 | Tropomyosin alpha-3 chainAdd BLAST | 284 | ||
| Isoform 2 (identifier: P06753-2) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / 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 | RemovedCombined 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>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
| ||||
| Isoform 3 (identifier: P06753-3) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / 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 | RemovedCombined 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>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
| ||||
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 | 2 | N-acetylmethionineBy 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 | 54 | PhosphothreonineBy 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 | 62 | PhosphoserineBy 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 | 88 | PhosphoserineCombined 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 | 109 | PhosphothreonineBy 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 | PhosphoserineBy 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 | 216 | PhosphoserineBy 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 | 253 | PhosphothreonineBy 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 | 262 | PhosphotyrosineBy 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 | 272 | PhosphoserineBy 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 | 283 | PhosphothreonineBy 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 | 284 | PhosphoserineBy 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 | ||
| Isoform 2 (identifier: P06753-2) | |||||
| <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-acetylalanineCombined 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>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 | 177 | N6-acetyllysineCombined 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>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 | 215 | N6-acetyllysineCombined 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>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 | ||
| Isoform 3 (identifier: P06753-3) | |||||
| <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-acetylalanineCombined 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>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 | 177 | N6-acetyllysineCombined 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>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 | ||
| Isoform 7 (identifier: P06753-7) | |||||
| <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 | 125 | N6-acetyllysineCombined 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 | ||
| Isoform 6 (identifier: P06753-6) | |||||
| <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 | 177 | N6-acetyllysineCombined 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 | ||
| Isoform 5 (identifier: P06753-5) | |||||
| <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 | 215 | N6-acetyllysineCombined 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>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 | P06753 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P06753 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P06753 |
PeptideAtlas More...PeptideAtlasi | P06753 |
PRoteomics IDEntifications database More...PRIDEi | P06753 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51930 51931 [P06753-2] 51932 [P06753-3] |
2D gel databases
DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEi | P06753 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P06753 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P06753 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P06753 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P06753 |
<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 | ENSG00000143549 |
CleanEx database of gene expression profiles More...CleanExi | HS_TPM3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P06753 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P06753 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA000261 HPA009066 HPA047089 HPA053624 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
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.14"Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene."
Sung L.A., Lin J.J.-C.
Biochem. Biophys. Res. Commun. 201:627-634(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TMOD1.
<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 |
|---|---|---|---|---|
| C1orf216 | Q8TAB5 | 3 | EBI-355607,EBI-747505 | |
| CCHCR1 | Q8TD31-3 | 11 | EBI-355607,EBI-10175300 | |
| FAM9C | Q8IZT9 | 5 | EBI-355607,EBI-2870039 | |
| HSF2 | Q03933 | 8 | EBI-355607,EBI-2556750 | |
| IFIT3 | O14879 | 5 | EBI-355607,EBI-745127 | |
| IKBKE | Q14164 | 2 | EBI-355607,EBI-307369 | |
| KXD1 | Q9BQD3 | 10 | EBI-355607,EBI-739657 | |
| LCA5L | O95447 | 3 | EBI-355607,EBI-8473670 | |
| LURAP1 | Q96LR2 | 3 | EBI-355607,EBI-741355 | |
| MAD1L1 | Q9Y6D9 | 9 | EBI-355607,EBI-742610 | |
| NUP54 | Q7Z3B4 | 4 | EBI-355607,EBI-741048 | |
| OIP5 | O43482 | 8 | EBI-355607,EBI-536879 | |
| SYCE1 | Q8N0S2 | 7 | EBI-355607,EBI-6872807 | |
| TFPT | A0A024R4Q5 | 6 | EBI-355607,EBI-11527449 | |
| TFPT | P0C1Z6 | 6 | EBI-355607,EBI-1245626 | |
| TFPT | P0C1Z6-2 | 3 | EBI-355607,EBI-10178002 | |
| THAP1 | Q9NVV9 | 4 | EBI-355607,EBI-741515 | |
| TNNT1 | P13805-3 | 3 | EBI-355607,EBI-12151635 | |
| VPS52 | Q8N1B4 | 3 | EBI-355607,EBI-2799833 |
<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
- actin filament binding Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 113023, 133 interactors |
Protein interaction database and analysis system More...IntActi | P06753, 75 interactors |
Molecular INTeraction database More...MINTi | P06753 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000357516 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P06753 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06753 |
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
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 1 – 285 | By similarityAdd BLAST | 285 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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
Coiled coilPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1003 Eukaryota ENOG410XR5K LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074494 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231522 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG107404 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06753 |
KEGG Orthology (KO) More...KOi | K09290 |
Identification of Orthologs from Complete Genome Data More...OMAi | EDRSKQH |
Database of Orthologous Groups More...OrthoDBi | EOG091G0UO7 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P06753 |
TreeFam database of animal gene trees More...TreeFami | TF351519 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000533 Tropomyosin |
Pfam protein domain database More...Pfami | View protein in Pfam PF00261 Tropomyosin, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00194 TROPOMYOSIN |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00326 TROPOMYOSIN, 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 (7)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 7 <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
MMEAIKKKMQ MLKLDKENAL DRAEQAEAEQ KQAEERSKQL EDELAAMQKK
60 70 80 90 100
LKGTEDELDK YSEALKDAQE KLELAEKKAA DAEAEVASLN RRIQLVEEEL
110 120 130 140 150
DRAQERLATA LQKLEEAEKA ADESERGMKV IENRALKDEE KMELQEIQLK
160 170 180 190 200
EAKHIAEEAD RKYEEVARKL VIIEGDLERT EERAELAESK CSELEEELKN
210 220 230 240 250
VTNNLKSLEA QAEKYSQKED KYEEEIKILT DKLKEAETRA EFAERSVAKL
260 270 280
EKTIDDLEDE LYAQKLKYKA ISEELDHALN DMTSI
The sequence of this isoform differs from the canonical sequence as follows:
1-81: MMEAIKKKMQ...LELAEKKAAD → MAGITTIEAV...VEGERRAREQ
190-212: KCSELEEELKNVTNNLKSLEAQA → RCREMDEQIRLMDQNLKCLSAAE
260-285: ELYAQKLKYKAISEELDHALNDMTSI → KLKCTKEEHLCTQRMLDQTLLDLNEM
10 20 30 40 50
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA
60 70 80 90 100
SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK
110 120 130 140 150
DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIEGDL ERTEERAELA
160 170 180 190 200
ESRCREMDEQ IRLMDQNLKC LSAAEEKYSQ KEDKYEEEIK ILTDKLKEAE
210 220 230 240
TRAEFAERSV AKLEKTIDDL EDKLKCTKEE HLCTQRMLDQ TLLDLNEM
<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
- Ref.17"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<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.10Cited for: PROTEIN SEQUENCE OF 93-119, PARTIAL PROTEIN SEQUENCE (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3), ACETYLATION AT ALA-2 (ISOFORMS 2/3), IDENTIFICATION BY MASS SPECTROMETRY.
<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
- Ref.17"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<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.10Cited for: PROTEIN SEQUENCE OF 93-119, PARTIAL PROTEIN SEQUENCE (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3), ACETYLATION AT ALA-2 (ISOFORMS 2/3), IDENTIFICATION BY MASS SPECTROMETRY.
The sequence of this isoform differs from the canonical sequence as follows:
1-81: MMEAIKKKMQ...LELAEKKAAD → MAGITTIEAV...VEGERRAREQ
190-212: KCSELEEELKNVTNNLKSLEAQA → RCREMDEQIRLMDQNLKCLSAAE
259-285: DELYAQKLKYKAISEELDHALNDMTSI → ERLYSQLERNRLLSNELKLTLHDLCD
10 20 30 40 50
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA
60 70 80 90 100
SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK
110 120 130 140 150
DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIEGDL ERTEERAELA
160 170 180 190 200
ESRCREMDEQ IRLMDQNLKC LSAAEEKYSQ KEDKYEEEIK ILTDKLKEAE
210 220 230 240
TRAEFAERSV AKLEKTIDDL EERLYSQLER NRLLSNELKL TLHDLCD
<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
- Ref.17"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<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.10Cited for: PROTEIN SEQUENCE OF 93-119, PARTIAL PROTEIN SEQUENCE (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3), ACETYLATION AT ALA-2 (ISOFORMS 2/3), IDENTIFICATION BY MASS SPECTROMETRY.
The sequence of this isoform differs from the canonical sequence as follows:
1-2: MM → MAGITTI
5-21: IKKKMQMLKLDKENALD → VKRKIQVLQQQADDAEE
25-81: QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD → RLQREVEGERRAREQ
259-260: DE → ER
263-285: AQKLKYKAISEELDHALNDMTSI → SQLERNRLLSNELKLTLHDLCD
10 20 30 40 50
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA
60 70 80 90 100
SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK
110 120 130 140 150
DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIEGDL ERTEERAELA
160 170 180 190 200
ESKCSELEEE LKNVTNNLKS LEAQAEKYSQ KEDKYEEEIK ILTDKLKEAE
210 220 230 240
TRAEFAERSV AKLEKTIDDL EERLYSQLER NRLLSNELKL TLHDLCD
The sequence of this isoform differs from the canonical sequence as follows:
1-2: MM → MAGITTI
5-21: IKKKMQMLKLDKENALD → VKRKIQVLQQQADDAEE
25-81: QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD → RLQREVEGERRAREQ
260-285: ELYAQKLKYKAISEELDHALNDMTSI → KLKCTKEEHLCTQRMLDQTLLDLNEM
10 20 30 40 50
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA
60 70 80 90 100
SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK
110 120 130 140 150
DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIEGDL ERTEERAELA
160 170 180 190 200
ESKCSELEEE LKNVTNNLKS LEAQAEKYSQ KEDKYEEEIK ILTDKLKEAE
210 220 230 240
TRAEFAERSV AKLEKTIDDL EDKLKCTKEE HLCTQRMLDQ TLLDLNEM
<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
- Ref.17"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
The sequence of this isoform differs from the canonical sequence as follows:
1-81: MMEAIKKKMQ...LELAEKKAAD → MAGITTIEAV...VEGERRAREQ
190-212: KCSELEEELKNVTNNLKSLEAQA → RCREMDEQIRLMDQNLKCLSAAE
10 20 30 40 50
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA
60 70 80 90 100
SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK
110 120 130 140 150
DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIEGDL ERTEERAELA
160 170 180 190 200
ESRCREMDEQ IRLMDQNLKC LSAAEEKYSQ KEDKYEEEIK ILTDKLKEAE
210 220 230 240
TRAEFAERSV AKLEKTIDDL EDELYAQKLK YKAISEELDH ALNDMTSI
<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
- Ref.17"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
The sequence of this isoform differs from the canonical sequence as follows:
1-127: Missing.
260-285: ELYAQKLKYKAISEELDHALNDMTSI → KLKCTKEEHLCTQRMLDQTLLDLNEM
10 20 30 40 50
MKVIENRALK DEEKMELQEI QLKEAKHIAE EADRKYEEVA RKLVIIEGDL
60 70 80 90 100
ERTEERAELA ESKCSELEEE LKNVTNNLKS LEAQAEKYSQ KEDKYEEEIK
110 120 130 140 150
ILTDKLKEAE TRAEFAERSV AKLEKTIDDL EDKLKCTKEE HLCTQRMLDQ
TLLDLNEM
<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
- Ref.17"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 150 | K → E in CAA27243 (PubMed:12574106).Curated | 1 | ||
| Isoform 2 (identifier: P06753-2) | |||||
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 33 | R → Q in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 43 | E → K in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 66 | A → P in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 85 | D → G in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 110 | I → L in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 135 | I → T in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 150 | A → T in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 192 | L → F in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 196 | L → P in ABC40673 (PubMed:16201836).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
<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 ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 202 | R → C in ABC40673 (PubMed:16201836).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
<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 | ||
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071499 | 4 | A → V in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_013460 | 9 | M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071500 | 88 | S → F in NEM1 and CAPM1. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071501 | 91 | R → C Probable disease-associated mutation found in patients with undefined congenital myopathy. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071502 | 91 | R → P in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070066 | 100 | L → M in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071503 | 100 | L → V in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071504 | 149 | L → I in CAPM1. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071505 | 151 | E → A in CAPM1. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070067 | 168 | R → C in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070068 | 168 | R → G in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070069 | 168 | R → H in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy. 6 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070070 | 169 | K → E in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071506 | 174 | E → A in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071507 | 241 | E → K in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070071 | 245 | R → G in CFTD. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071508 | 245 | R → I in CAPM1. 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071509 | 253 | T → K Probable disease-associated mutation found in patients with undefined congenital myopathy. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_054792 | 1 – 127 | Missing in isoform 7. CuratedAdd BLAST | 127 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006604 | 1 – 81 | MMEAI…KKAAD → MAGITTIEAVKRKIQVLQQQ ADDAEERAERLQREVEGERR AREQ in isoform 2, isoform 3 and isoform 6. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 81 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047302 | 1 – 2 | MM → MAGITTI in isoform 4 and isoform 5. Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047303 | 5 – 21 | IKKKM…ENALD → VKRKIQVLQQQADDAEE in isoform 4 and isoform 5. CuratedAdd BLAST | 17 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047304 | 25 – 81 | QAEAE…KKAAD → RLQREVEGERRAREQ in isoform 4 and isoform 5. CuratedAdd BLAST | 57 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006605 | 190 – 212 | KCSEL…LEAQA → RCREMDEQIRLMDQNLKCLS AAE in isoform 2, isoform 3 and isoform 6. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 23 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006607 | 259 – 285 | DELYA…DMTSI → ERLYSQLERNRLLSNELKLT LHDLCD in isoform 3. CuratedAdd BLAST | 27 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047305 | 259 – 260 | DE → ER in isoform 4. Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006606 | 260 – 285 | ELYAQ…DMTSI → KLKCTKEEHLCTQRMLDQTL LDLNEM in isoform 2, isoform 5 and isoform 7. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 26 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047306 | 263 – 285 | AQKLK…DMTSI → SQLERNRLLSNELKLTLHDL CD in isoform 4. CuratedAdd BLAST | 23 |
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 | X04201 mRNA Translation: CAA27798.1 AY004867 mRNA Translation: AAF87083.1 X04588 mRNA Translation: CAB37185.1 AL590431 Genomic DNA No translation available. CH471121 Genomic DNA Translation: EAW53229.1 CH471121 Genomic DNA Translation: EAW53230.1 CH471121 Genomic DNA Translation: EAW53231.1 CH471121 Genomic DNA Translation: EAW53235.1 BC000771 mRNA Translation: AAH00771.1 BC008407 mRNA Translation: AAH08407.1 BC008425 mRNA Translation: AAH08425.1 BC015403 mRNA Translation: AAH15403.1 BC072428 mRNA Translation: AAH72428.1 DQ120714 Genomic DNA Translation: ABC40673.1 X03541 mRNA Translation: CAA27243.1 Different termination. AF474157 mRNA Translation: AAL84570.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1060.1 [P06753-2] CCDS41400.1 [P06753-5] CCDS41401.1 [P06753-4] CCDS41402.1 [P06753-3] CCDS41403.1 [P06753-1] CCDS60274.1 [P06753-7] CCDS60275.1 [P06753-6] |
Protein sequence database of the Protein Information Resource More...PIRi | A25530 S06210 A24199 |
NCBI Reference Sequences More...RefSeqi | NP_001036816.1, NM_001043351.1 [P06753-5] NP_001036817.1, NM_001043352.1 [P06753-3] NP_001036818.1, NM_001043353.1 [P06753-4] NP_001265118.1, NM_001278189.1 [P06753-6] NP_001265120.1, NM_001278191.1 [P06753-7] NP_689476.2, NM_152263.3 [P06753-1] NP_705935.1, NM_153649.3 [P06753-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.535581 Hs.578978 Hs.644306 Hs.654421 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000302206; ENSP00000307712; ENSG00000143549 [P06753-7] ENST00000323144; ENSP00000357518; ENSG00000143549 [P06753-4] ENST00000328159; ENSP00000357520; ENSG00000143549 [P06753-6] ENST00000330188; ENSP00000339035; ENSG00000143549 [P06753-5] ENST00000368530; ENSP00000357516; ENSG00000143549 [P06753-1] ENST00000368531; ENSP00000357517; ENSG00000143549 [P06753-3] ENST00000368533; ENSP00000357521; ENSG00000143549 [P06753-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 7170 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:7170 |
UCSC genome browser More...UCSCi | uc001fdy.2 human [P06753-1] |
<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, Chromosomal rearrangement<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 | |
|---|---|---|---|---|---|
| P06753 | TPM3 isoform 2 | 285 | |||
| Tropomyosin alpha-3 chain | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| +20 | |||||
| P06753-2 | Tropomyosin alpha-3 chain isoform 2 | 248 | |||
| Tropomyosin 3 isoform 1 (Fragment) | 248 | ||||
| Tropomyosin alpha-3 chain isoform 2 | 248 | ||||
| TPM3 isoform 13 | 248 | ||||
| tropomyosin alpha-3 chain isoform X1 | 248 | ||||
| +10 | |||||
| P06753-3 | TPM3 isoform 16 | 247 | |||
| Tropomyosin 3 | 247 | ||||
| Uncharacterized protein | 247 | ||||
| TPM3 isoform 14 | 247 | ||||
| Uncharacterized protein | 247 | ||||
| +9 | |||||
| P06753-4 | TPM3 isoform 14 | 247 | |||
| Tropomyosin 3 | 247 | ||||
| Tropomyosin alpha-3 chain isoform 5 | 247 | ||||
| Tropomyosin 3 | 247 | ||||
| Uncharacterized protein | 247 | ||||
| +8 | |||||
| P06753-5 | Tropomyosin alpha-3 chain isoform 4 | 248 | |||
| Tropomyosin 3 isoform 3 (Fragment) | 248 | ||||
| Tropomyosin 3 | 248 | ||||
| TPM3 isoform 6 | 248 | ||||
| tropomyosin alpha-3 chain isoform X6 | 248 | ||||
| +9 | |||||
| P06753-6 | TPM3 isoform 17 | 248 | |||
| tropomyosin alpha-3 chain isoform X7 | 248 | ||||
| Tropomyosin 3 | 248 | ||||
| Tropomyosin 3 | 248 | ||||
| Tropomyosin 3 | 248 | ||||
| +15 | |||||
| P06753-7 | Tropomyosin alpha-3 chain isoform 1 | 287 | |||
| tropomyosin alpha-3 chain isoform X15 | 158 | ||||
| TPM3 isoform 13 | 158 | ||||
| TPM3 isoform 19 | 158 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P06753 | TPM3 isoform 2 | 285 | |||
| Tropomyosin alpha-3 chain | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| +87 | |||||
| P06753-2 | Tropomyosin alpha-3 chain | 248 | |||
| UPI0005F56B75 | 286 | ||||
| UPI0003F0D451 | 261 | ||||
| UPI0004402072 | 261 | ||||
| Uncharacterized protein | 253 | ||||
| +88 | |||||
| P06753-3 | TPM3 isoform 16 | 247 | |||
| Tropomyosin 3 | 247 | ||||
| Uncharacterized protein | 247 | ||||
| TPM3 isoform 14 | 247 | ||||
| Uncharacterized protein | 247 | ||||
| +38 | |||||
| P06753-4 | Tropomyosin alpha-3 chain | 306 | |||
| UPI00053FD4A1 | 248 | ||||
| UPI0000F2BCC1 | 248 | ||||
| UPI0003D75AF1 | 248 | ||||
| UPI0004D0AAE8 | 248 | ||||
| +75 | |||||
| P06753-5 | Tropomyosin alpha-3 chain | 306 | |||
| UPI00053FD4A1 | 248 | ||||
| UPI0000F2BCC1 | 248 | ||||
| UPI0003D75AF1 | 248 | ||||
| UPI0004D0AAE8 | 248 | ||||
| +75 | |||||
| P06753-6 | UPI000154FED1 | 254 | |||
| Uncharacterized protein | 296 | ||||
| UPI000B3D8FE5 | 296 | ||||
| UPI00071A7694 | 294 | ||||
| UPI000395DBBB | 248 | ||||
| +143 | |||||
| P06753-7 | Tropomyosin alpha-3 chain isoform 1 | 287 | |||
| tropomyosin alpha-3 chain isoform X15 | 158 | ||||
| TPM3 isoform 13 | 158 | ||||
| TPM3 isoform 19 | 158 | ||||
| Tropomyosin alpha-3 chain isoform 1 | 287 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P06753 | TPM3 isoform 2 | 285 | |||
| Tropomyosin alpha-3 chain | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| Tropomyosin 3 | 285 | ||||
| +1103 | |||||
| P06753-2 | UPI00044329B4 | 286 | |||
| UPI0009819C0F | 277 | ||||
| UPI000952185C | 262 | ||||
| UPI000C9DAFE9 | 262 | ||||
| UPI0004D04F73 | 251 | ||||
| +1261 | |||||
| P06753-3 | UPI00044329B4 | 286 | |||
| UPI0009819C0F | 277 | ||||
| UPI000952185C | 262 | ||||
| UPI000C9DAFE9 | 262 | ||||
| UPI0004D04F73 | 251 | ||||
| +1261 | |||||
| P06753-4 | UPI00044329B4 | 286 | |||
| UPI0009819C0F | 277 | ||||
| UPI000952185C | 262 | ||||
| UPI000C9DAFE9 | 262 | ||||
| UPI0004D04F73 | 251 | ||||
| +1261 | |||||
| P06753-5 | UPI00044329B4 | 286 | |||
| UPI0009819C0F | 277 | ||||
| UPI000952185C | 262 | ||||
| UPI000C9DAFE9 | 262 | ||||
| UPI0004D04F73 | 251 | ||||
| +1261 | |||||
| P06753-6 | UPI00044329B4 | 286 | |||
| UPI0009819C0F | 277 | ||||
| UPI000952185C | 262 | ||||
| UPI000C9DAFE9 | 262 | ||||
| UPI0004D04F73 | 251 | ||||
| +1261 | |||||
| P06753-7 | LOC535277 protein | 284 | |||
| Uncharacterized protein | 285 | ||||
| tropomyosin alpha-1 chain-like isoform X1 | 284 | ||||
| UPI00034FE960 | 284 | ||||
| UPI0007F918C9 | 284 | ||||
| +466 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
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 | X04201 mRNA Translation: CAA27798.1 AY004867 mRNA Translation: AAF87083.1 X04588 mRNA Translation: CAB37185.1 AL590431 Genomic DNA No translation available. CH471121 Genomic DNA Translation: EAW53229.1 CH471121 Genomic DNA Translation: EAW53230.1 CH471121 Genomic DNA Translation: EAW53231.1 CH471121 Genomic DNA Translation: EAW53235.1 BC000771 mRNA Translation: AAH00771.1 BC008407 mRNA Translation: AAH08407.1 BC008425 mRNA Translation: AAH08425.1 BC015403 mRNA Translation: AAH15403.1 BC072428 mRNA Translation: AAH72428.1 DQ120714 Genomic DNA Translation: ABC40673.1 X03541 mRNA Translation: CAA27243.1 Different termination. AF474157 mRNA Translation: AAL84570.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1060.1 [P06753-2] CCDS41400.1 [P06753-5] CCDS41401.1 [P06753-4] CCDS41402.1 [P06753-3] CCDS41403.1 [P06753-1] CCDS60274.1 [P06753-7] CCDS60275.1 [P06753-6] |
Protein sequence database of the Protein Information Resource More...PIRi | A25530 S06210 A24199 |
NCBI Reference Sequences More...RefSeqi | NP_001036816.1, NM_001043351.1 [P06753-5] NP_001036817.1, NM_001043352.1 [P06753-3] NP_001036818.1, NM_001043353.1 [P06753-4] NP_001265118.1, NM_001278189.1 [P06753-6] NP_001265120.1, NM_001278191.1 [P06753-7] NP_689476.2, NM_152263.3 [P06753-1] NP_705935.1, NM_153649.3 [P06753-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.535581 Hs.578978 Hs.644306 Hs.654421 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P06753 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06753 |
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 | 113023, 133 interactors |
Protein interaction database and analysis system More...IntActi | P06753, 75 interactors |
Molecular INTeraction database More...MINTi | P06753 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000357516 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P06753 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P06753 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P06753 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 519668659 |
2D gel databases
DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEi | P06753 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P06753 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P06753 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P06753 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P06753 |
PeptideAtlas More...PeptideAtlasi | P06753 |
PRoteomics IDEntifications database More...PRIDEi | P06753 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51930 51931 [P06753-2] 51932 [P06753-3] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000302206; ENSP00000307712; ENSG00000143549 [P06753-7] ENST00000323144; ENSP00000357518; ENSG00000143549 [P06753-4] ENST00000328159; ENSP00000357520; ENSG00000143549 [P06753-6] ENST00000330188; ENSP00000339035; ENSG00000143549 [P06753-5] ENST00000368530; ENSP00000357516; ENSG00000143549 [P06753-1] ENST00000368531; ENSP00000357517; ENSG00000143549 [P06753-3] ENST00000368533; ENSP00000357521; ENSG00000143549 [P06753-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 7170 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:7170 |
UCSC genome browser More...UCSCi | uc001fdy.2 human [P06753-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 7170 |
DisGeNET More...DisGeNETi | 7170 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000143549.19 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TPM3 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | TPM3 |
Human Gene Nomenclature Database More...HGNCi | HGNC:12012 TPM3 |
Human Protein Atlas More...HPAi | HPA000261 HPA009066 HPA047089 HPA053624 |
MalaCards human disease database More...MalaCardsi | TPM3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 164970 gene 191030 gene 255310 phenotype 609284 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P06753 |
Open Targets More...OpenTargetsi | ENSG00000143549 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 171881 Cap myopathy 171439 Childhood-onset nemaline myopathy 2020 Congenital fiber-type disproportion myopathy 178342 Inflammatory myofibroblastic tumor 171433 Intermediate nemaline myopathy |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36692 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1003 Eukaryota ENOG410XR5K LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074494 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231522 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG107404 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06753 |
KEGG Orthology (KO) More...KOi | K09290 |
Identification of Orthologs from Complete Genome Data More...OMAi | EDRSKQH |
Database of Orthologous Groups More...OrthoDBi | EOG091G0UO7 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P06753 |
TreeFam database of animal gene trees More...TreeFami | TF351519 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-390522 Striated Muscle Contraction R-HSA-445355 Smooth Muscle Contraction |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | TPM3 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Tropomyosin_3 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 7170 |
Protein Ontology More...PROi | PR:P06753 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000143549 |
CleanEx database of gene expression profiles More...CleanExi | HS_TPM3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P06753 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P06753 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000533 Tropomyosin |
Pfam protein domain database More...Pfami | View protein in Pfam PF00261 Tropomyosin, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00194 TROPOMYOSIN |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00326 TROPOMYOSIN, 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 | TPM3_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 | P06753Primary (citable) accession number: P06753 Secondary accession number(s): D3DV71 , P12324, Q2QD06, Q5VU58, Q5VU63, Q5VU66, Q5VU71, Q5VU72, Q8TCG3, Q969Q2, Q9NQH8 | |
| <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 1, 1988 |
| Last sequence update: | June 26, 2013 | |
| Last modified: | July 18, 2018 | |
| This is version 209 of the entry and version 2 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
Complete proteome, Direct protein sequencing, 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 - SIMILARITY comments
Index of protein domains and families
