UniProtKB - Q5T4F4 (ZFY27_HUMAN)
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- BLAST>sp|Q5T4F4|ZFY27_HUMAN Protrudin OS=Homo sapiens GN=ZFYVE27 PE=1 SV=1 MQTSEREGSGPELSPSVMPEAPLESPPFPTKSPAFDLFNLVLSYKRLEIYLEPLKDAGDG VRYLLRWQMPLCSLLTCLGLNVLFLTLNEGAWYSVGALMISVPALLGYLQEVCRARLPDS ELMRRKYHSVRQEDLQRGRLSRPEAVAEVKSFLIQLEAFLSRLCCTCEAAYRVLHWENPV VSSQFYGALLGTVCMLYLLPLCWVLTLLNSTLFLGNVEFFRVVSEYRASLQQRMNPKQEE HAFESPPPPDVGGKDGLMDSTPALTPTEDLTPGSVEEAEEAEPDEEFKDAIEETHLVVLE DDEGAPCPAEDELALQDNGFLSKNEVLRSKVSRLTERLRKRYPTNNFGNCTGCSATFSVL KKRRSCSNCGNSFCSRCCSFKVPKSSMGATAPEAQRETVFVCASCNQTLSK
- Align
Protein
Protrudin
Gene
ZFYVE27
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport (PubMed:17082457). Promotes axonal elongation and contributes to the establishment of neuronal cell polarity (By similarity). Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner (PubMed:19289470). Contributes to both the formation and stabilization of the tubular ER network (PubMed:24668814). Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections (PubMed:23969831). Acts as an adapter protein and facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (PubMed:21976701).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
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.5"Protrudin induces neurite formation by directional membrane trafficking."
Shirane M., Nakayama K.I.
Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FKBP8 AND RAB11A, PHOSPHORYLATION, MUTAGENESIS OF LEU-13 AND ILE-49. - Ref.7"Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA AND VAPB, MUTAGENESIS OF ASP-289, SUBCELLULAR LOCATION. - Ref.8"Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation."
Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.
Mol. Biol. Cell 22:4602-4620(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KIF5A; VAPA; VAPB AND RTN3. - Ref.12"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST. - Ref.13"Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia."
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REEP1; REEP5 AND ATL1.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 344 – 410 | FYVE-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 67 |
<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
- metal ion binding Source: UniProtKB-KW
- protein self-association Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- endoplasmic reticulum tubular network formation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- neuron projection development Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neurotrophin TRK receptor signaling pathway Source: UniProtKB
- positive regulation of axon extension Source: UniProtKB
- protein localization to plasma membrane Source: UniProtKB
- vesicle-mediated transport Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>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
| Ligand | Metal-binding, Zinc |
<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 ‘Names and Taxonomy’ 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: ProtrudinAlternative name(s): Spastic paraplegia 33 protein1 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
Zinc finger FYVE domain-containing protein 27 |
| <p>This subsection of the ‘Names and taxonomy’ 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:ZFYVE27 Synonyms:SPG331 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 ‘Names and taxonomy’ 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 ‘Names and taxonomy’ section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the ‘Names and taxonomy’ 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 “Names and Taxonomy” 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:ENSG00000155256.17. |
Human Gene Nomenclature Database More...HGNCi | HGNC:26559. ZFYVE27. |
<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
Endosome
- Recycling endosome membrane 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
; Multi-pass membrane protein Sequence analysis
- Recycling endosome membrane By similarity
Plasma membrane
- growth cone membrane 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
; Multi-pass membrane protein Sequence analysis
- growth cone membrane By similarity
Endoplasmic reticulum
- Endoplasmic reticulum membrane 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.7"Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA AND VAPB, MUTAGENESIS OF ASP-289, SUBCELLULAR LOCATION. - Ref.12"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST. - Ref.13"Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia."
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REEP1; REEP5 AND ATL1.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.12"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST.
Note: Localizes at both dendrites and axons (By similarity). Localizes to endoplasmic reticulum tubular network.By similarity- Endoplasmic reticulum membrane 3 Publications
- Ref.12"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST. - Ref.13"Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia."
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REEP1; REEP5 AND ATL1.
<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
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
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endoplasmic reticulum tubular network Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- integral component of endoplasmic reticulum membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Endosome
- recycling endosome membrane Source: UniProtKB
Plasma Membrane
- growth cone membrane Source: UniProtKB
Other locations
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 – 66 | 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
| 66 | |
| <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 | 67 – 87 | HelicalSequence analysisAdd BLAST | 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 | 88 | Lumenal1 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/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 | 89 – 109 | HelicalSequence analysisAdd BLAST | 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 | 110 – 187 | 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
| 78 | |
| <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 | 188 – 208 | HelicalSequence analysisAdd BLAST | 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 | 209 – 411 | 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
| 203 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cell projection, Endoplasmic reticulum, Endosome, 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
<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"><span class="caps">OMIM</span></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
Spastic paraplegia 33, autosomal dominant (SPG33)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.10"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia."
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG33 VAL-191, CHARACTERIZATION OF VARIANT SPG33 VAL-191, SUBCELLULAR LOCATION, INTERACTION WITH SPAST. - Ref.11"The role of ZFYVE27/protrudin in hereditary spastic paraplegia."
Martignoni M., Riano E., Rugarli E.I.
Am. J. Hum. Genet. 83:127-130(2008) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191. - Ref.12"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST. - Ref.13"Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia."
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REEP1; REEP5 AND ATL1.
Ref.10
"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia."
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG33 VAL-191, CHARACTERIZATION OF VARIANT SPG33 VAL-191, SUBCELLULAR LOCATION, INTERACTION WITH SPAST.
Ref.11
"The role of ZFYVE27/protrudin in hereditary spastic paraplegia."
Martignoni M., Riano E., Rugarli E.I.
Am. J. Hum. Genet. 83:127-130(2008) [PubMed] [Europe PMC] [Abstract]
Martignoni M., Riano E., Rugarli E.I.
Am. J. Hum. Genet. 83:127-130(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191.
Ref.12
"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST.
Ref.13
"Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia."
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REEP1; REEP5 AND ATL1.
The disease is caused by mutations affecting the gene represented in this entry. According to PubMed:18606302, the properties of the variant Val-191 and its frequency in some populations raise doubts on the implication of that gene in the disease.
Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
See also OMIM:610244| 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_027269 | 191 | G → V in SPG33; no effect on its function in the regulation of ER morphology and stability, no effect on its localization to ER but according to PubMed:16826525 an aberrant subcellular localization to cell membrane seen, altered interaction with SPAST, increased susceptibility to ER stress, no effect on its interaction with REEP1, REEP5 and ATL1 and increased protein stabilty. 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
| 1 |
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 | 13 | L → A: Alters interaction with RAB11A; when associated with A-49. 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 | 49 | I → A: Alters interaction with RAB11A; when associated with A-13. 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 | 289 | D → A: Loss of interaction with VAPA and loss of function in cell projections formation. 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, Hereditary spastic paraplegia, NeurodegenerationOrganism-specific databases
DisGeNET More...DisGeNETi | 118813. |
MalaCards human disease database More...MalaCardsi | ZFYVE27. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 610244. phenotype. |
Open Targets More...OpenTargetsi | ENSG00000155256. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134863310. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ZFYVE27. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74744927. |
<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_0000245601 | 1 – 411 | ProtrudinAdd BLAST | 411 |
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"><span class="caps">PTM</span> / 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 | 209 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/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
Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A.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.5"Protrudin induces neurite formation by directional membrane trafficking."
Shirane M., Nakayama K.I.
Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FKBP8 AND RAB11A, PHOSPHORYLATION, MUTAGENESIS OF LEU-13 AND ILE-49.
<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
Glycoprotein, PhosphoproteinProteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | Q5T4F4. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q5T4F4. |
PeptideAtlas More...PeptideAtlasi | Q5T4F4. |
PRoteomics IDEntifications database More...PRIDEi | Q5T4F4. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q5T4F4. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q5T4F4. |
<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 | ENSG00000155256. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q5T4F4. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA037523. HPA069876. |
<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
Can form homooligomers (monomers, dimers and tetramers) (PubMed:23969831). Interacts with RAB11A (GDP-bound form); regulates RAB11A (PubMed:17082457). Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation (PubMed:17082457, PubMed:18459960). Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation (PubMed:19289470, PubMed:21976701). Interacts with VAPB (via MSP domain) (PubMed:19289470, PubMed:21976701). Interacts with REEP1, REEP5 and ATL1 (PubMed:24668814, PubMed:23969831). Interacts with ATL2, ATL3 and SPAST (PubMed:23969831). Interacts with KIF5A and RTN3 (PubMed:21976701). Interacts with RAB11B (GDP-bound form), SURF4, KIF5B and KIF5C (By similarity).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
7 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"Protrudin induces neurite formation by directional membrane trafficking."
Shirane M., Nakayama K.I.
Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FKBP8 AND RAB11A, PHOSPHORYLATION, MUTAGENESIS OF LEU-13 AND ILE-49. - Ref.6"Regulation of apoptosis and neurite extension by FKBP38 is required for neural tube formation in the mouse."
Shirane M., Ogawa M., Motoyama J., Nakayama K.I.
Genes Cells 13:635-651(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FKBP8. - Ref.7"Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA AND VAPB, MUTAGENESIS OF ASP-289, SUBCELLULAR LOCATION. - Ref.8"Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation."
Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.
Mol. Biol. Cell 22:4602-4620(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KIF5A; VAPA; VAPB AND RTN3. - Ref.10"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia."
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG33 VAL-191, CHARACTERIZATION OF VARIANT SPG33 VAL-191, SUBCELLULAR LOCATION, INTERACTION WITH SPAST. - Ref.12"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST. - Ref.13"Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia."
Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T., Nakayama K.I.
J. Biol. Chem. 289:12946-12961(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REEP1; REEP5 AND ATL1.
<p>This subsection of the ‘Interaction’ 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 |
|---|---|---|---|---|
| FKBP8 | Q14318 | 4 | EBI-3892947,EBI-724839 | |
| RAB11A | P62491 | 4 | EBI-3892947,EBI-745098 | |
| VAPA | Q9P0L0 | 5 | EBI-3892947,EBI-1059156 | |
| VAPB | O95292 | 2 | EBI-3892947,EBI-1188298 |
<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
- protein self-association Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 125623. 23 interactors. |
The comprehensive resource of mammalian protein complexes More...CORUMi | Q5T4F4. |
Database of interacting proteins More...DIPi | DIP-61530N. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q5T4F4. |
Protein interaction database and analysis system More...IntActi | Q5T4F4. 7 interactors. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000348593. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 351 – 353 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 359 – 361 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 367 – 369 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 375 – 377 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 380 – 382 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 385 – 387 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 399 – 401 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 403 – 410 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 |
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 |
| 1X4U | NMR | - | A | 341-411 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q5T4F4. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q5T4F4. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q5T4F4. |
<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 | 1 – 205 | Sufficient for localization to endoplasmic reticulum tubular network and for interactions with REEP1, REEP5, ATL1, ATL2, ATL3 and SPAST2 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
| 205 | |
| <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 | 1 – 92 | Sufficient for homooligomerization1 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
| 92 | |
| <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 | 51 – 64 | Necessary for interaction with RAB11A and function in neurite outgrowth1 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
| 14 | |
| <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 | 271 – 361 | Necessary for interaction with KIF5A1 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
| 91 | |
| <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 | 286 – 292 | Necessary for interaction with VAPA and function in cell projections formation | 7 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 246 – 249 | Poly-Pro | 4 |
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 344 – 410 | FYVE-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 67 |
<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 helix, Zinc-fingerPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IJBT. Eukaryota. ENOG4111KCR. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00390000013298. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000155785. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054907. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q5T4F4. |
KEGG Orthology (KO) More...KOi | K19368. |
Identification of Orthologs from Complete Genome Data More...OMAi | RCCSFKV. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0QCA. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q5T4F4. |
TreeFam database of animal gene trees More...TreeFami | TF331044. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.40.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. |
Pfam protein domain database More...Pfami | View protein in Pfam PF01363. FYVE. 1 hit. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00064. FYVE. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57903. SSF57903. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50178. ZF_FYVE. 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 length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8)i
<p>This subsection of the ‘Sequence’ 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 8 <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
Isoform 1 (identifier: Q5T4F4-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY
60 70 80 90 100
LEPLKDAGDG VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI
110 120 130 140 150
SVPALLGYLQ EVCRARLPDS ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK
160 170 180 190 200
SFLIQLEAFL SRLCCTCEAA YRVLHWENPV VSSQFYGALL GTVCMLYLLP
210 220 230 240 250
LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE HAFESPPPPD
260 270 280 290 300
VGGKDGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEETHLVVLE
310 320 330 340 350
DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGNC
360 370 380 390 400
TGCSATFSVL KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF
410
VCASCNQTLS K
Length:411
Mass (Da):45,843
Last modified:December 21, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i5B86C64A398033D2
Isoform 2 (identifier: Q5T4F4-2) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
294-300: Missing.
10 20 30 40 50
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY
60 70 80 90 100
LEPLKDAGDG VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI
110 120 130 140 150
SVPALLGYLQ EVCRARLPDS ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK
160 170 180 190 200
SFLIQLEAFL SRLCCTCEAA YRVLHWENPV VSSQFYGALL GTVCMLYLLP
210 220 230 240 250
LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE HAFESPPPPD
260 270 280 290 300
VGGKDGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEEDDEGAPC
310 320 330 340 350
PAEDELALQD NGFLSKNEVL RSKVSRLTER LRKRYPTNNF GNCTGCSATF
360 370 380 390 400
SVLKKRRSCS NCGNSFCSRC CSFKVPKSSM GATAPEAQRE TVFVCASCNQ
TLSK
Length:404
Mass (Da):45,052
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0FA0436DAE7716D7
Isoform 3 (identifier: Q5T4F4-3) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
268-268: E → ESLSSQ
10 20 30 40 50
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY
60 70 80 90 100
LEPLKDAGDG VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI
110 120 130 140 150
SVPALLGYLQ EVCRARLPDS ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK
160 170 180 190 200
SFLIQLEAFL SRLCCTCEAA YRVLHWENPV VSSQFYGALL GTVCMLYLLP
210 220 230 240 250
LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE HAFESPPPPD
260 270 280 290 300
VGGKDGLMDS TPALTPTESL SSQDLTPGSV EEAEEAEPDE EFKDAIEETH
310 320 330 340 350
LVVLEDDEGA PCPAEDELAL QDNGFLSKNE VLRSKVSRLT ERLRKRYPTN
360 370 380 390 400
NFGNCTGCSA TFSVLKKRRS CSNCGNSFCS RCCSFKVPKS SMGATAPEAQ
410
RETVFVCASC NQTLSK
Length:416
Mass (Da):46,346
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iBF488D2456C6B924
Isoform 4 (identifier: Q5T4F4-4) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
1-68: Missing.
268-268: E → ESLSSQ
294-300: Missing.
349-356: NCTGCSAT → VTGAGSS
357-411: Missing.
10 20 30 40 50
MPLCSLLTCL GLNVLFLTLN EGAWYSVGAL MISVPALLGY LQEVCRARLP
60 70 80 90 100
DSELMRRKYH SVRQEDLQRG RLSRPEAVAE VKSFLIQLEA FLSRLCCTCE
110 120 130 140 150
AAYRVLHWEN PVVSSQFYGA LLGTVCMLYL LPLCWVLTLL NSTLFLGNVE
160 170 180 190 200
FFRVVSEYRA SLQQRMNPKQ EEHAFESPPP PDVGGKDGLM DSTPALTPTE
210 220 230 240 250
SLSSQDLTPG SVEEAEEAEP DEEFKDAIEE DDEGAPCPAE DELALQDNGF
260 270 280
LSKNEVLRSK VSRLTERLRK RYPTNNFGVT GAGSS
Length:285
Mass (Da):31,744
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i977E99E1E5857BDD
Isoform 5 (identifier: Q5T4F4-5) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
66-152: RWQMPLCSLL...PEAVAEVKSF → S
294-300: Missing.
10 20 30 40 50
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY
60 70 80 90 100
LEPLKDAGDG VRYLLSLIQL EAFLSRLCCT CEAAYRVLHW ENPVVSSQFY
110 120 130 140 150
GALLGTVCML YLLPLCWVLT LLNSTLFLGN VEFFRVVSEY RASLQQRMNP
160 170 180 190 200
KQEEHAFESP PPPDVGGKDG LMDSTPALTP TEDLTPGSVE EAEEAEPDEE
210 220 230 240 250
FKDAIEEDDE GAPCPAEDEL ALQDNGFLSK NEVLRSKVSR LTERLRKRYP
260 270 280 290 300
TNNFGNCTGC SATFSVLKKR RSCSNCGNSF CSRCCSFKVP KSSMGATAPE
310
AQRETVFVCA SCNQTLSK
Length:318
Mass (Da):35,205
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1E3E1DF487779DEB
Isoform 6 (identifier: Q5T4F4-6) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
67-184: Missing.
294-300: Missing.
10 20 30 40 50
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY
60 70 80 90 100
LEPLKDAGDG VRYLLRFYGA LLGTVCMLYL LPLCWVLTLL NSTLFLGNVE
110 120 130 140 150
FFRVVSEYRA SLQQRMNPKQ EEHAFESPPP PDVGGKDGLM DSTPALTPTE
160 170 180 190 200
DLTPGSVEEA EEAEPDEEFK DAIEEDDEGA PCPAEDELAL QDNGFLSKNE
210 220 230 240 250
VLRSKVSRLT ERLRKRYPTN NFGNCTGCSA TFSVLKKRRS CSNCGNSFCS
260 270 280
RCCSFKVPKS SMGATAPEAQ RETVFVCASC NQTLSK
Note: No experimental confirmation available.
Show »Length:286
Mass (Da):31,612
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iC4F817D0A286151B
Isoform 7 (identifier: Q5T4F4-7) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-98: Missing.
268-268: E → ESLSSQ
294-300: Missing.
10 20 30 40 50
MISVPALLGY LQEVCRARLP DSELMRRKYH SVRQEDLQRG RLSRPEAVAE
60 70 80 90 100
VKSFLIQLEA FLSRLCCTCE AAYRVLHWEN PVVSSQFYGA LLGTVCMLYL
110 120 130 140 150
LPLCWVLTLL NSTLFLGNVE FFRVVSEYRA SLQQRMNPKQ EEHAFESPPP
160 170 180 190 200
PDVGGKDGLM DSTPALTPTE SLSSQDLTPG SVEEAEEAEP DEEFKDAIEE
210 220 230 240 250
DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGNC
260 270 280 290 300
TGCSATFSVL KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF
310
VCASCNQTLS K
Note: No experimental confirmation available.
Show »Length:311
Mass (Da):34,681
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i3035EAF2EF4EEA53
Isoform 8 (identifier: Q5T4F4-8) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
58-89: Missing.
294-300: Missing.
10 20 30 40 50
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY
60 70 80 90 100
LEPLKDAGAW YSVGALMISV PALLGYLQEV CRARLPDSEL MRRKYHSVRQ
110 120 130 140 150
EDLQRGRLSR PEAVAEVKSF LIQLEAFLSR LCCTCEAAYR VLHWENPVVS
160 170 180 190 200
SQFYGALLGT VCMLYLLPLC WVLTLLNSTL FLGNVEFFRV VSEYRASLQQ
210 220 230 240 250
RMNPKQEEHA FESPPPPDVG GKDGLMDSTP ALTPTEDLTP GSVEEAEEAE
260 270 280 290 300
PDEEFKDAIE EDDEGAPCPA EDELALQDNG FLSKNEVLRS KVSRLTERLR
310 320 330 340 350
KRYPTNNFGN CTGCSATFSV LKKRRSCSNC GNSFCSRCCS FKVPKSSMGA
360 370
TAPEAQRETV FVCASCNQTL SK
Note: No experimental confirmation available.
Show »Length:372
Mass (Da):41,417
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0D235A6E1A98B2E2
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence CAD38913 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
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 | 50 | Y → N in AAH30621 (PubMed:15489334).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 218 | E → G in BAC11260 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 222 | V → F in BAH13112 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 340 | K → R in BAH13112 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 387 | M → A in BAH13112 (PubMed:14702039).Curated | 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_027002 | 82 | V → I. Corresponds to variant dbSNP:rs17108378Ensembl. | 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_027003 | 138 | G → V3 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_027269 | 191 | G → V in SPG33; no effect on its function in the regulation of ER morphology and stability, no effect on its localization to ER but according to PubMed:16826525 an aberrant subcellular localization to cell membrane seen, altered interaction with SPAST, increased susceptibility to ER stress, no effect on its interaction with REEP1, REEP5 and ATL1 and increased protein stabilty. 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
| 1 |
Alternative sequence
Sequence databases
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000337540; ENSP00000337993; ENSG00000155256. [Q5T4F4-8] ENST00000357540; ENSP00000350148; ENSG00000155256. [Q5T4F4-5] ENST00000359980; ENSP00000353069; ENSG00000155256. [Q5T4F4-2] ENST00000370610; ENSP00000359642; ENSG00000155256. [Q5T4F4-7] ENST00000370613; ENSP00000359646; ENSG00000155256. [Q5T4F4-6] ENST00000393677; ENSP00000377282; ENSG00000155256. [Q5T4F4-1] ENST00000423811; ENSP00000409594; ENSG00000155256. [Q5T4F4-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 118813. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:118813. |
UCSC genome browser More...UCSCi | uc001kol.3. human. [Q5T4F4-1] |
<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, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
|---|---|---|---|---|---|---|---|
| Q5T4F4 | A0A0S2Z627 | Homo sapiens (Human) | 411 | UniRef100_Q5T4F4 | Cluster: Protrudin | 2 | |
| Q5T4F4-2 | A0A0S2Z5V0 | Homo sapiens (Human) | 404 | UniRef100_Q5T4F4-2 | Cluster: Isoform 2 of Protrudin | 2 |
<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
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 |
| 1X4U | NMR | - | A | 341-411 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q5T4F4. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q5T4F4. | |||||
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 | 125623. 23 interactors. |
The comprehensive resource of mammalian protein complexes More...CORUMi | Q5T4F4. |
Database of interacting proteins More...DIPi | DIP-61530N. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q5T4F4. |
Protein interaction database and analysis system More...IntActi | Q5T4F4. 7 interactors. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000348593. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q5T4F4. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q5T4F4. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ZFYVE27. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74744927. |
Proteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | Q5T4F4. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q5T4F4. |
PeptideAtlas More...PeptideAtlasi | Q5T4F4. |
PRoteomics IDEntifications database More...PRIDEi | Q5T4F4. |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000337540; ENSP00000337993; ENSG00000155256. [Q5T4F4-8] ENST00000357540; ENSP00000350148; ENSG00000155256. [Q5T4F4-5] ENST00000359980; ENSP00000353069; ENSG00000155256. [Q5T4F4-2] ENST00000370610; ENSP00000359642; ENSG00000155256. [Q5T4F4-7] ENST00000370613; ENSP00000359646; ENSG00000155256. [Q5T4F4-6] ENST00000393677; ENSP00000377282; ENSG00000155256. [Q5T4F4-1] ENST00000423811; ENSP00000409594; ENSG00000155256. [Q5T4F4-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 118813. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:118813. |
UCSC genome browser More...UCSCi | uc001kol.3. human. [Q5T4F4-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 118813. |
DisGeNET More...DisGeNETi | 118813. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000155256.17. |
GeneCards: human genes, protein and diseases More...GeneCardsi | ZFYVE27. |
Human Gene Nomenclature Database More...HGNCi | HGNC:26559. ZFYVE27. |
Human Protein Atlas More...HPAi | HPA037523. HPA069876. |
MalaCards human disease database More...MalaCardsi | ZFYVE27. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 610243. gene. 610244. phenotype. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q5T4F4. |
Open Targets More...OpenTargetsi | ENSG00000155256. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134863310. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IJBT. Eukaryota. ENOG4111KCR. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00390000013298. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000155785. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054907. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q5T4F4. |
KEGG Orthology (KO) More...KOi | K19368. |
Identification of Orthologs from Complete Genome Data More...OMAi | RCCSFKV. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0QCA. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q5T4F4. |
TreeFam database of animal gene trees More...TreeFami | TF331044. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | ZFYVE27. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q5T4F4. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 118813. |
Protein Ontology More...PROi | PR:Q5T4F4. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000155256. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q5T4F4. HS. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.40.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. |
Pfam protein domain database More...Pfami | View protein in Pfam PF01363. FYVE. 1 hit. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00064. FYVE. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57903. SSF57903. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50178. ZF_FYVE. 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 | ZFY27_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 | Q5T4F4Primary (citable) accession number: Q5T4F4 Secondary accession number(s): B7Z3S0 , B7Z404, B7Z626, G8JLC3, G8JLF0, J3KP98, Q5T4F1, Q5T4F2, Q5T4F3, Q8N1K0, Q8N6D6, Q8NCA0, Q8NDE4, Q96M08 | |
| <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 11, 2006 |
| Last sequence update: | December 21, 2004 | |
| Last modified: | September 27, 2017 | |
| This is version 132 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 10
Human chromosome 10: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references