UniProtKB - Q8TDD5 (MCLN3_HUMAN)
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- BLAST>sp|Q8TDD5|MCLN3_HUMAN Mucolipin-3 OS=Homo sapiens OX=9606 GN=MCOLN3 PE=1 SV=1 MADPEVVVSSCSSHEEENRCNFNQQTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKP WKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQS DVYDQLIFAVNQYLQLYNVSVGNHAYENKGTKQSAMAICQHFYKRGNIYPGNDTFDIDPE IETECFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYD FTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHYMMIFDAFVILTCLVSL ILCIRSVIRGLQLQQEFVNFFLLHYKKEVSVSDQMEFVNGWYIMIIISDILTIIGSILKM EIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAA MIYLGYCFCGWIVLGPYHDKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRI YLYSFISLFIYMILSLFIALITDTYETIKQYQQDGFPETELRTFISECKDLPNSGKYRLE DDPPVSLFCCCKK
- Align
Mucolipin-3
MCOLN3
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
Curated8 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.4"A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype."
Kim H.J., Li Q., Tjon-Kon-Sang S., So I., Kiselyov K., Soyombo A.A., Muallem S.
EMBO J. 27:1197-1205(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-252; HIS-273; HIS-283 AND ALA-419. - Ref.5"The calcium channel mucolipin-3 is a novel regulator of trafficking along the endosomal pathway."
Martina J.A., Lelouvier B., Puertollano R.
Traffic 10:1143-1156(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459. - Ref.7"Properties of the TRPML3 channel pore and its stable expansion by the Varitint-Waddler-causing mutation."
Kim H.J., Yamaguchi S., Li Q., So I., Muallem S.
J. Biol. Chem. 285:16513-16520(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-283; ALA-419; GLU-449 AND ASP-459. - Ref.8"Functional multimerization of mucolipin channel proteins."
Curcio-Morelli C., Zhang P., Venugopal B., Charles F.A., Browning M.F., Cantiello H.F., Slaugenhaupt S.A.
J. Cell. Physiol. 222:328-335(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, FUNCTION. - Ref.9"Mucolipin-3 regulates luminal calcium, acidification, and membrane fusion in the endosomal pathway."
Lelouvier B., Puertollano R.
J. Biol. Chem. 286:9826-9832(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.10"A novel ion channel formed by interaction of TRPML3 with TRPV5."
Guo Z., Grimm C., Becker L., Ricci A.J., Heller S.
PLoS ONE 8:E58174-E58174(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.11"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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.4"A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype."
Kim H.J., Li Q., Tjon-Kon-Sang S., So I., Kiselyov K., Soyombo A.A., Muallem S.
EMBO J. 27:1197-1205(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-252; HIS-273; HIS-283 AND ALA-419. - Ref.7"Properties of the TRPML3 channel pore and its stable expansion by the Varitint-Waddler-causing mutation."
Kim H.J., Yamaguchi S., Li Q., So I., Muallem S.
J. Biol. Chem. 285:16513-16520(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-283; ALA-419; GLU-449 AND ASP-459. - Ref.11"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- calcium channel activity Source: Reactome
- lipid binding Source: UniProtKB-KW
<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
- calcium ion transmembrane transport Source: Reactome
- inner ear auditory receptor cell differentiation Source: Ensembl
- locomotory behavior Source: Ensembl
<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 | Ion channel |
| Biological process | Ion transport, Transport |
| Ligand | Lipid-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3295583 TRP channels |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.A.5.3.4 the polycystin cation channel (pcc) family |
<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: Mucolipin-31 Publication<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
Alternative name(s): Transient receptor potential channel mucolipin 3 Short name: TRPML31 Publication <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
|
| <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:MCOLN3 |
| <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:ENSG00000055732.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:13358 MCOLN3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607400 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8TDD5 |
<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
Lysosome
- Lysosome membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459.
<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"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
- Lysosome membrane 1 Publication
Endosome
- Early endosome membrane 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"The calcium channel mucolipin-3 is a novel regulator of trafficking along the endosomal pathway."
Martina J.A., Lelouvier B., Puertollano R.
Traffic 10:1143-1156(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459.
<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"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
- Late endosome membrane 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"The calcium channel mucolipin-3 is a novel regulator of trafficking along the endosomal pathway."
Martina J.A., Lelouvier B., Puertollano R.
Traffic 10:1143-1156(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459.
<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"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
- Early endosome membrane 2 Publications
Plasma membrane
- Cell membrane 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459. - Ref.11"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
<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"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
- Cell membrane 2 Publications
Other locations
- autophagosome membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459.
Note: Recycles between the plasma membrane and intracellular compartments by a dynamin-dependent endocytic pathway (PubMed:19522758). Under normal conditions, only a very minor proportion is present at the cell membrane (PubMed:19522758). In the cochlea located at the base of stereocilia near the position of the ankle links (By similarity).By similarity- autophagosome membrane 1 Publication
- Ref.6"The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy."
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.
Traffic 10:1157-1167(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-458 AND 458-ASP-ASP-459.
<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
Endosome
- early endosome membrane Source: UniProtKB-SubCell
- late endosome membrane Source: UniProtKB-SubCell
Lysosome
- lysosomal membrane Source: UniProtKB-SubCell
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- autophagosome membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 62 | Cytoplasmic1 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
| 62 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 63 – 83 | Helical1 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 84 – 283 | Extracellular1 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
| 200 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 284 – 304 | Helical1 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 305 – 341 | Cytoplasmic1 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
| 37 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 342 – 362 | Helical1 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 363 – 371 | Extracellular1 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
| 9 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 372 – 392 | Helical1 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 393 – 414 | Cytoplasmic1 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
| 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 415 – 435 | Helical1 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 436 – 443 | Extracellular1 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
| 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei | 444 – 464 | Pore-forming1 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 465 – 475 | Extracellular1 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
| 11 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 476 – 497 | Helical1 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
| 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 498 – 553 | Cytoplasmic1 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
| 56 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cytoplasmic vesicle, Endosome, Lysosome, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 108 | D → N: Abolishes basal channel activity without affecting channel activation by a synthetic agonist; when associated with N-111 and N-112. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 111 | D → N: Abolishes basal channel activity without affecting channel activation by a synthetic agonist; when associated with N-108 and N-112. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 112 | D → N: Abolishes basal channel activity without affecting channel activation by a synthetic agonist; when associated with N-108 and N-111. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 252 | H → A: Increases inhibition by lumenal H(+). Decreases inhibition by lumenal H(+); when associated with A-283. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 273 | H → A: Increases inhibition by lumenal H(+). Decreases inhibition by lumenal H(+); when associated with A-283. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 283 | H → A: Constitutive active channel; abolishes inhibition by lumenal H(+); retains the Ca(2+)-dependent inactivation of the Ca(2+) current. Decreases inhibition by lumenal H(+); when associated with A-252. Decreases inhibition by lumenal H(+); when associated with A-273. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 283 | H → R: Increases inhibition by lumenal H(+). 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 419 | A → P: Constitutive active channel; abolishes inhibition by lumenal H(+); increases the pore diameter. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 423 | Y → A: Nearly abolishes channel activation by a synthetic agonist. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 449 | E → A: Constitutive active channel; greatly impairs inhibition by lumenal Na(+). 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 449 | E → K: Abolishes channel activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 458 – 459 | DD → KK: Enhances endocytosis. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 458 | D → K: Nearly abolishes channel activity; inhibits starvation-induced autophagy. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 459 | D → A: Decreases in Ca(2+) permeability and selectivity; decreases channel pore dynamic behavior. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 497 | F → A: Nearly abolishes channel activation by a synthetic agonist. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 55283 |
Open Targets More...OpenTargetsi | ENSG00000055732 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134947324 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1293243 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 503 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MCOLN3 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 50401084 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000215367 | 1 – 553 | Mucolipin-3Add BLAST | 553 |
Amino acid modifications
| 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 specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 138 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 159 ↔ 185 | By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 172 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 205 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 238 ↔ 269 | By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Functional multimerization of mucolipin channel proteins."
Curcio-Morelli C., Zhang P., Venugopal B., Charles F.A., Browning M.F., Cantiello H.F., Slaugenhaupt S.A.
J. Cell. Physiol. 222:328-335(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, FUNCTION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8TDD5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8TDD5 |
PeptideAtlas More...PeptideAtlasi | Q8TDD5 |
PRoteomics IDEntifications database More...PRIDEi | Q8TDD5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 74270 74271 [Q8TDD5-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8TDD5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8TDD5 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q8TDD5 |
<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 | ENSG00000055732 |
CleanEx database of gene expression profiles More...CleanExi | HS_MCOLN3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8TDD5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8TDD5 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA018106 HPA062137 |
<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 which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.10"A novel ion channel formed by interaction of TRPML3 with TRPV5."
Guo Z., Grimm C., Becker L., Ricci A.J., Heller S.
PLoS ONE 8:E58174-E58174(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Functional multimerization of mucolipin channel proteins."
Curcio-Morelli C., Zhang P., Venugopal B., Charles F.A., Browning M.F., Cantiello H.F., Slaugenhaupt S.A.
J. Cell. Physiol. 222:328-335(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, FUNCTION. - Ref.11"Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states."
Zhou X., Li M., Su D., Jia Q., Li H., Li X., Yang J.
Nat. Struct. Mol. Biol. 24:1146-1154(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.62 ANGSTROMS), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION AT ASN-138 AND ASN-172, MUTAGENESIS OF ASP-108; ASP-111; ASP-112; TYR-423 AND PHE-497.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 305 | Interaction with phosphoinositidesBy 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 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 120571, 60 interactors |
Protein interaction database and analysis system More...IntActi | Q8TDD5, 1 interactor |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000304843 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q8TDD5 |
<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
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 6AYE | electron microscopy | 4.06 | A/B/C/D | 1-553 | [»] | |
| 6AYF | electron microscopy | 3.62 | A/B/C/D | 1-553 | [»] | |
| 6AYG | electron microscopy | 4.65 | A/B/C/D | 1-553 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q8TDD5 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8TDD5 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 52 – 62 | Interaction with phosphoinositidesBy 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 Add BLAST | 11 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 104 – 118 | Extracellular/lumenal pore loopBy 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 Add BLAST | 15 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 456 – 459 | Selectivity filter1 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
| 4 |
<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>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 ‘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
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3733 Eukaryota ENOG410Z1HH LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000017126 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000232158 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052430 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8TDD5 |
KEGG Orthology (KO) More...KOi | K04994 |
Identification of Orthologs from Complete Genome Data More...OMAi | HEEENRC |
Database of Orthologous Groups More...OrthoDBi | EOG091G026A |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8TDD5 |
TreeFam database of animal gene trees More...TreeFami | TF317783 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR013122 PKD1_2_channel |
Pfam protein domain database More...Pfami | View protein in Pfam PF08016 PKD_channel, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MADPEVVVSS CSSHEEENRC NFNQQTSPSE ELLLEDQMRR KLKFFFMNPC
60 70 80 90 100
EKFWARGRKP WKLAIQILKI AMVTIQLVLF GLSNQMVVAF KEENTIAFKH
110 120 130 140 150
LFLKGYMDRM DDTYAVYTQS DVYDQLIFAV NQYLQLYNVS VGNHAYENKG
160 170 180 190 200
TKQSAMAICQ HFYKRGNIYP GNDTFDIDPE IETECFFVEP DEPFHIGTPA
210 220 230 240 250
ENKLNLTLDF HRLLTVELQF KLKAINLQTV RHQELPDCYD FTLTITFDNK
260 270 280 290 300
AHSGRIKISL DNDISIRECK DWHVSGSIQK NTHYMMIFDA FVILTCLVSL
310 320 330 340 350
ILCIRSVIRG LQLQQEFVNF FLLHYKKEVS VSDQMEFVNG WYIMIIISDI
360 370 380 390 400
LTIIGSILKM EIQAKSLTSY DVCSILLGTS TMLVWLGVIR YLGFFAKYNL
410 420 430 440 450
LILTLQAALP NVIRFCCCAA MIYLGYCFCG WIVLGPYHDK FRSLNMVSEC
460 470 480 490 500
LFSLINGDDM FATFAKMQQK SYLVWLFSRI YLYSFISLFI YMILSLFIAL
510 520 530 540 550
ITDTYETIKQ YQQDGFPETE LRTFISECKD LPNSGKYRLE DDPPVSLFCC
CKK
The sequence of this isoform differs from the canonical sequence as follows:
77-132: Missing.
10 20 30 40 50
MADPEVVVSS CSSHEEENRC NFNQQTSPSE ELLLEDQMRR KLKFFFMNPC
60 70 80 90 100
EKFWARGRKP WKLAIQILKI AMVTIQYLQL YNVSVGNHAY ENKGTKQSAM
110 120 130 140 150
AICQHFYKRG NIYPGNDTFD IDPEIETECF FVEPDEPFHI GTPAENKLNL
160 170 180 190 200
TLDFHRLLTV ELQFKLKAIN LQTVRHQELP DCYDFTLTIT FDNKAHSGRI
210 220 230 240 250
KISLDNDISI RECKDWHVSG SIQKNTHYMM IFDAFVILTC LVSLILCIRS
260 270 280 290 300
VIRGLQLQQE FVNFFLLHYK KEVSVSDQME FVNGWYIMII ISDILTIIGS
310 320 330 340 350
ILKMEIQAKS LTSYDVCSIL LGTSTMLVWL GVIRYLGFFA KYNLLILTLQ
360 370 380 390 400
AALPNVIRFC CCAAMIYLGY CFCGWIVLGP YHDKFRSLNM VSECLFSLIN
410 420 430 440 450
GDDMFATFAK MQQKSYLVWL FSRIYLYSFI SLFIYMILSL FIALITDTYE
460 470 480 490
TIKQYQQDGF PETELRTFIS ECKDLPNSGK YRLEDDPPVS LFCCCKK
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 | 9 | S → C in BAA91951 (PubMed:14702039).Curated | 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF475085 mRNA Translation: AAL84622.1 AK001868 mRNA Translation: BAA91951.1 AL358789 Genomic DNA No translation available. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS58009.1 [Q8TDD5-2] CCDS701.1 [Q8TDD5-1] |
NCBI Reference Sequences More...RefSeqi | NP_001240622.1, NM_001253693.1 [Q8TDD5-2] NP_060768.8, NM_018298.10 [Q8TDD5-1] XP_005271060.1, XM_005271003.1 [Q8TDD5-1] XP_006710813.1, XM_006710750.1 [Q8TDD5-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.535239 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000341115; ENSP00000342698; ENSG00000055732 [Q8TDD5-2] ENST00000370589; ENSP00000359621; ENSG00000055732 [Q8TDD5-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55283 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55283 |
UCSC genome browser More...UCSCi | uc001dkp.4 human [Q8TDD5-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q8TDD5 | UPI0007DC66B5 | 566 | |||
| Mucolipin 3 | 577 | ||||
| UPI000642E254 | 576 | ||||
| UPI0006982F48 | 569 | ||||
| UPI000BDFB0AD | 561 | ||||
| +72 | |||||
| Q8TDD5-2 | UPI0005D018CF | 521 | |||
| UPI000D532B32 | 523 | ||||
| MCOLN3 isoform 3 | 497 | ||||
| Mucolipin 3 | 497 | ||||
| Mucolipin 3 | 497 | ||||
| +30 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q8TDD5 | UPI0007DC66B5 | 566 | |||
| Mucolipin 3 | 577 | ||||
| UPI000642E254 | 576 | ||||
| UPI0006982F48 | 569 | ||||
| UPI000BDFB0AD | 561 | ||||
| +536 | |||||
| Q8TDD5-2 | UPI0005D018CF | 521 | |||
| UPI000D532B32 | 523 | ||||
| Mucolipin 3 | 497 | ||||
| UPI0003C102D4 | 497 | ||||
| UPI000B5356CB | 497 | ||||
| +91 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF475085 mRNA Translation: AAL84622.1 AK001868 mRNA Translation: BAA91951.1 AL358789 Genomic DNA No translation available. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS58009.1 [Q8TDD5-2] CCDS701.1 [Q8TDD5-1] |
NCBI Reference Sequences More...RefSeqi | NP_001240622.1, NM_001253693.1 [Q8TDD5-2] NP_060768.8, NM_018298.10 [Q8TDD5-1] XP_005271060.1, XM_005271003.1 [Q8TDD5-1] XP_006710813.1, XM_006710750.1 [Q8TDD5-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.535239 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 6AYE | electron microscopy | 4.06 | A/B/C/D | 1-553 | [»] | |
| 6AYF | electron microscopy | 3.62 | A/B/C/D | 1-553 | [»] | |
| 6AYG | electron microscopy | 4.65 | A/B/C/D | 1-553 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q8TDD5 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8TDD5 | |||||
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 | 120571, 60 interactors |
Protein interaction database and analysis system More...IntActi | Q8TDD5, 1 interactor |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000304843 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q8TDD5 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1293243 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 503 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.A.5.3.4 the polycystin cation channel (pcc) family |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8TDD5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8TDD5 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q8TDD5 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MCOLN3 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 50401084 |
Proteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8TDD5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8TDD5 |
PeptideAtlas More...PeptideAtlasi | Q8TDD5 |
PRoteomics IDEntifications database More...PRIDEi | Q8TDD5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 74270 74271 [Q8TDD5-2] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000341115; ENSP00000342698; ENSG00000055732 [Q8TDD5-2] ENST00000370589; ENSP00000359621; ENSG00000055732 [Q8TDD5-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55283 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55283 |
UCSC genome browser More...UCSCi | uc001dkp.4 human [Q8TDD5-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 55283 |
DisGeNET More...DisGeNETi | 55283 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000055732.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MCOLN3 |
Human Gene Nomenclature Database More...HGNCi | HGNC:13358 MCOLN3 |
Human Protein Atlas More...HPAi | HPA018106 HPA062137 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607400 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8TDD5 |
Open Targets More...OpenTargetsi | ENSG00000055732 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134947324 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3733 Eukaryota ENOG410Z1HH LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000017126 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000232158 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052430 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8TDD5 |
KEGG Orthology (KO) More...KOi | K04994 |
Identification of Orthologs from Complete Genome Data More...OMAi | HEEENRC |
Database of Orthologous Groups More...OrthoDBi | EOG091G026A |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8TDD5 |
TreeFam database of animal gene trees More...TreeFami | TF317783 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3295583 TRP channels |
Miscellaneous databases
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MCOLN3 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 55283 |
Protein Ontology More...PROi | PR:Q8TDD5 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000055732 |
CleanEx database of gene expression profiles More...CleanExi | HS_MCOLN3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8TDD5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8TDD5 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR013122 PKD1_2_channel |
Pfam protein domain database More...Pfami | View protein in Pfam PF08016 PKD_channel, 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 | MCLN3_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 | Q8TDD5Primary (citable) accession number: Q8TDD5 Secondary accession number(s): Q5T4H5, Q5T4H6, Q9NV09 | |
| <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: | July 19, 2004 |
| Last sequence update: | June 1, 2002 | |
| Last modified: | June 20, 2018 | |
| This is version 130 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
