UniProtKB - Q86YS7 (C2CD5_HUMAN)
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- BLAST>sp|Q86YS7|C2CD5_HUMAN C2 domain-containing protein 5 OS=Homo sapiens OX=9606 GN=C2CD5 PE=1 SV=1 MPGKLKVKIVAGRHLPVMDRASDLTDAFVEVKFGNTTFKTDVYLKSLNPQWNSEWFKFEV DDEDLQDEPLQITVLDHDTYSANDAIGKVYIDIDPLLYSEAATVISGWFPIYDTIHGIRG EINVVVKVDLFNDLNRFRQSSCGVKFFCTTSIPKCYRAVIIHGFVEELVVNEDPEYQWID RIRTPRASNEARQRLISLMSGELQRKIGLKVLEMRGNAVVGYLQCFDLEGESGLVVRAIG TACTLDKLSSPAAFLPACNSPSKEMKEIPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSY SRQSSSSDTDLSLTPKTGMGSGSAGKEGGPFKALLRQQTQSALEQREFPFFTLTAFPPGF LVHVGGVVSARSVKLLDRIHNPDEPETRDAWWAEIRQEIKSHAKALGCHAVVGYSESTSI CEEVCILSASGTAAVLNPRFLQDGTVEGCLEQRLEENLPTRCGFCHIPYDELNMPFPAHL TYCYNCRKQKVPDVLFTTIDLPTDATVIGKGCLIQARLCRLKKKAQAEANATAISNLLPF MEYEVHTQLMNKLKLKGMNALFGLRIQITVGENMLMGLASATGVYLAALPTPGGIQIAGK TPNDGSYEQHISHMQKKINDTIAKNKELYEINPPEISEEIIGSPIPEPRQRSRLLRSQSE SSDEVTELDLSHGKKDAFVLEIDDTDAMEDVHSLLTDVPPPSGFYSCNTEIMPGINNWTS EIQMFTSVRVIRLSSLNLTNQALNKNFNDLCENLLKSLYFKLRSMIPCCLCHVNFTVSLP EDELIQVTVTAVAITFDKNQALQTTKTPVEKSLQRASTDNEELLQFPLELCSDSLPSHPF PPAKAMTVEKASPVGDGNFRNRSAPPCANSTVGVVKMTPLSFIPGAKITKYLGIINMFFI RETTSLREEGGVSGFLHAFIAEVFAMVRAHVAALGGNAVVSYIMKQCVFMENPNKNQAQC LINVSGDAVVFVRESDLEVVSSQQPTTNCQSSCTEGEVTT
- Align
Protein
C2 domain-containing protein 5
Gene
C2CD5
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. 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
Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM.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.16"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Ca2+Note: Binds 2 calcium ions per subunit. The ions are bound to the C2 domains.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi | 13 – 27 | 1; low affinityAdd BLAST | 15 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi | 75 – 86 | 2; high affinityAdd BLAST | 12 |
<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-dependent phospholipid binding 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
- calcium ion binding 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
- cellular response to insulin stimulus 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
- insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
- intracellular protein transmembrane transport 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
- positive regulation of glucose import in response to insulin stimulus Source: Ensembl
- positive regulation of glucose transmembrane transport Source: UniProtKB
- positive regulation of protein targeting to membrane 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
- positive regulation of vesicle fusion 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
- protein localization to plasma membrane Source: Ensembl
- vesicle fusion 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
| Biological process | Protein transport, Transport |
| Ligand | Calcium, Lipid-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1445148 Translocation of GLUT4 to the plasma membrane |
<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: C2 domain-containing protein 5Alternative name(s): C2 domain-containing phosphoprotein of 138 kDa |
| <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:C2CD5 Synonyms:CDP138, KIAA0528 |
| <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:ENSG00000111731.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:29062 C2CD5 |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q86YS7 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
- Cell membrane 1 Publication
Other locations
- Cytoplasmic vesicle 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.16"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
- cell cortex 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.16"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
- ruffle 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.16"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
Note: Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation.- Cytoplasmic vesicle membrane 1 Publication
Cytoskeleton
- microtubule organizing center Source: HPA
Cytosol
- cytosol Source: HPA
Plasma Membrane
- plasma 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
- ruffle 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
Other locations
- cell cortex 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
- cytoplasmic vesicle 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
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, 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 | 19 | D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-26; A-76; A-78 and A-84. 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 | 26 | D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-76; A-78 and A-84. 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 | 76 | D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-78 and A-84. 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 | 78 | D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-84. 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 | 84 | D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-78. 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 | 197 | S → A: Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion. 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 | 200 | S → A: Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation. 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
Open Targets More...OpenTargetsi | ENSG00000111731 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA143485515 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 74750574 |
<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_0000247450 | 1 – 1000 | C2 domain-containing protein 5Add BLAST | 1000 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 197 | Phosphoserine; by PKB/AKT21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 200 | Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 260 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 293 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 295 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 304 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 305 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 306 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 317 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 323 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 601 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 643 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 657 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 659 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 661 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 662 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 666 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 671 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 807 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 817 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 852 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <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
Phosphorylated on Ser-197 by active myristoylated kinase AKT2; insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4 translocation into the plasma 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.16"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
<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
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q86YS7 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q86YS7 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q86YS7 |
PeptideAtlas More...PeptideAtlasi | Q86YS7 |
PRoteomics IDEntifications database More...PRIDEi | Q86YS7 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 70464 70465 [Q86YS7-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q86YS7 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q86YS7 |
<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 | ENSG00000111731 |
CleanEx database of gene expression profiles More...CleanExi | HS_KIAA0528 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q86YS7 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q86YS7 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA046194 |
<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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115182, 38 interactors |
Protein interaction database and analysis system More...IntActi | Q86YS7, 22 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000334229 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q86YS7 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q86YS7 |
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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1 – 90 | C2PROSITE-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 | 90 |
<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
The C2 domain binds to calcium and membrane lipids.
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1031 Eukaryota ENOG410XQDE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000000212 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000006746 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG081824 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q86YS7 |
Identification of Orthologs from Complete Genome Data More...OMAi | CANSTVG |
Database of Orthologous Groups More...OrthoDBi | EOG091G0FX6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q86YS7 |
TreeFam database of animal gene trees More...TreeFami | TF323431 |
Family and domain databases
Conserved Domains Database More...CDDi | cd08688 C2_KIAA0528-like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.150, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037785 C2_C2CD5 IPR000008 C2_dom IPR035892 C2_domain_sf IPR038983 C2CD5 |
The PANTHER Classification System More...PANTHERi | PTHR37412 PTHR37412, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00168 C2, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00239 C2, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50004 C2, 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 (5)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 5 <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: Q86YS7-1) [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
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ
60 70 80 90 100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE
110 120 130 140 150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT
160 170 180 190 200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS
210 220 230 240 250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS
260 270 280 290 300
PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
310 320 330 340 350
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF
360 370 380 390 400
FTLTAFPPGF LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK
410 420 430 440 450
SHAKALGCHA VVGYSESTSI CEEVCILSAS GTAAVLNPRF LQDGTVEGCL
460 470 480 490 500
EQRLEENLPT RCGFCHIPYD ELNMPFPAHL TYCYNCRKQK VPDVLFTTID
510 520 530 540 550
LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF MEYEVHTQLM
560 570 580 590 600
NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK
610 620 630 640 650
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ
660 670 680 690 700
RSRLLRSQSE SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP
710 720 730 740 750
PSGFYSCNTE IMPGINNWTS EIQMFTSVRV IRLSSLNLTN QALNKNFNDL
760 770 780 790 800
CENLLKSLYF KLRSMIPCCL CHVNFTVSLP EDELIQVTVT AVAITFDKNQ
810 820 830 840 850
ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF PPAKAMTVEK
860 870 880 890 900
ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI
910 920 930 940 950
RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM
960 970 980 990 1000
ENPNKNQAQC LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT
Length:1,000
Mass (Da):110,447
Last modified:June 1, 2003 - 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:i7C51961F54CBBACD
Isoform 2 (identifier: Q86YS7-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT
10 20 30 40 50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ
60 70 80 90 100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE
110 120 130 140 150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT
160 170 180 190 200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS
210 220 230 240 250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS
260 270 280 290 300
PAAFLPACNS PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV
310 320 330 340 350
SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQREFP FFTLTAFPPG
360 370 380 390 400
FLVHVGGVVS ARSVKLLDRI HNPDEPETRD AWWAEIRQEI KSHAKALGCH
410 420 430 440 450
AVVGYSESTS ICEEVCILSA SGTAAVLNPR FLQDGTVEGC LEQRLEENLP
460 470 480 490 500
TRCGFCHIPY DELNMPFPAH LTYCYNCRKQ KVPDVLFTTI DLPTDATVIG
510 520 530 540 550
KGCLIQARLC RLKKKAQAEA NATAISNLLP FMEYEVHTQL MNKLKLKGMN
560 570 580 590 600
ALFGLRIQIT VGENMLMGLA SATGVYLAAL PTPGGIQIAG KTPNDGSYEQ
610 620 630 640 650
HISHMQKKIN DTIAKNKELY EINPPEISEE IIGSPIPEPR QRSRLLRSQS
660 670 680 690 700
ESSDEVTELD LSHGKKDAFV LEIDDTDAME DVHSLLTDVP PPSGFYSCNT
710 720 730 740 750
EIMPGINNWT SEIQMFTSVR VIRLSSLNLT NQALNKNFND LCENLLKSLY
760 770 780 790 800
FKLRSMIPCC LCHVNFTVSL PEDELIQVTV TAVAITFDKN QALQTTKTPV
810 820 830 840 850
EKSLQRASTD NEELLQFPLE LCSDSLPSHP FPPAKEHLES ASSNSGIPAA
860 870 880 890 900
QRATSVDYSS FADRCSSWIE LIKLKAQTIR RGSIKTTMTV EKASPVGDGN
910 920 930 940 950
FRNRSAPPCA NSTVGVVKMT PLSFIPGAKI TKYLGIINMF FIRETTSLRE
960 970 980 990 1000
EGGVSGFLHA FIAEVFAMVR AHVAALGGNA VVSYIMKQCV FMENPNKNQA
1010 1020 1030 1040
QCLINVSGDA VVFVRESDLE VVSSQQPTTN CQSSCTEGEV TT
Note: No experimental confirmation available.
Show »Length:1,042
Mass (Da):114,994
<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:i23C91754C1A61236
Isoform 3 (identifier: Q86YS7-3) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT
10 20 30 40 50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ
60 70 80 90 100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE
110 120 130 140 150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT
160 170 180 190 200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS
210 220 230 240 250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS
260 270 280 290 300
PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
310 320 330 340 350
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF
360 370 380 390 400
FTLTAFPPGF LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK
410 420 430 440 450
SHAKALGCHA VVGYSESTSI CEEVCILSAS GTAAVLNPRF LQDGTVEGCL
460 470 480 490 500
EQRLEENLPT RCGFCHIPYD ELNMPFPAHL TYCYNCRKQK VPDVLFTTID
510 520 530 540 550
LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF MEYEVHTQLM
560 570 580 590 600
NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK
610 620 630 640 650
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ
660 670 680 690 700
RSRLLRSQSE SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP
710 720 730 740 750
PSGFYSCNTE IMPGINNWTS EIQMFTSVRV IRLSSLNLTN QALNKNFNDL
760 770 780 790 800
CENLLKSLYF KLRSMIPCCL CHVNFTVSLP EDELIQVTVT AVAITFDKNQ
810 820 830 840 850
ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF PPAKEHLESA
860 870 880 890 900
SSNSGIPAAQ RATSVDYSSF ADRCSSWIEL IKLKAQTIRR GSIKTTMTVE
910 920 930 940 950
KASPVGDGNF RNRSAPPCAN STVGVVKMTP LSFIPGAKIT KYLGIINMFF
960 970 980 990 1000
IRETTSLREE GGVSGFLHAF IAEVFAMVRA HVAALGGNAV VSYIMKQCVF
1010 1020 1030 1040 1050
MENPNKNQAQ CLINVSGDAV VFVRESDLEV VSSQQPTTNC QSSCTEGEVT
T
Note: No experimental confirmation available.
Show »Length:1,051
Mass (Da):116,027
<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:i2C4D059D41F01BE8
Isoform 4 (identifier: Q86YS7-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
345-345: Q → QRGGSPHRFCRR
845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT
10 20 30 40 50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ
60 70 80 90 100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE
110 120 130 140 150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT
160 170 180 190 200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS
210 220 230 240 250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS
260 270 280 290 300
PAAFLPACNS PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV
310 320 330 340 350
SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQRGGS PHRFCRRREF
360 370 380 390 400
PFFTLTAFPP GFLVHVGGVV SARSVKLLDR IHNPDEPETR DAWWAEIRQE
410 420 430 440 450
IKSHAKALGC HAVVGYSEST SICEEVCILS ASGTAAVLNP RFLQDGTVEG
460 470 480 490 500
CLEQRLEENL PTRCGFCHIP YDELNMPFPA HLTYCYNCRK QKVPDVLFTT
510 520 530 540 550
IDLPTDATVI GKGCLIQARL CRLKKKAQAE ANATAISNLL PFMEYEVHTQ
560 570 580 590 600
LMNKLKLKGM NALFGLRIQI TVGENMLMGL ASATGVYLAA LPTPGGIQIA
610 620 630 640 650
GKTPNDGSYE QHISHMQKKI NDTIAKNKEL YEINPPEISE EIIGSPIPEP
660 670 680 690 700
RQRSRLLRSQ SESSDEVTEL DLSHGKKDAF VLEIDDTDAM EDVHSLLTDV
710 720 730 740 750
PPPSGFYSCN TEIMPGINNW TSEIQMFTSV RVIRLSSLNL TNQALNKNFN
760 770 780 790 800
DLCENLLKSL YFKLRSMIPC CLCHVNFTVS LPEDELIQVT VTAVAITFDK
810 820 830 840 850
NQALQTTKTP VEKSLQRAST DNEELLQFPL ELCSDSLPSH PFPPAKEHLE
860 870 880 890 900
SASSNSGIPA AQRATSVDYS SFADRCSSWI ELIKLKAQTI RRGSIKTTMT
910 920 930 940 950
VEKASPVGDG NFRNRSAPPC ANSTVGVVKM TPLSFIPGAK ITKYLGIINM
960 970 980 990 1000
FFIRETTSLR EEGGVSGFLH AFIAEVFAMV RAHVAALGGN AVVSYIMKQC
1010 1020 1030 1040 1050
VFMENPNKNQ AQCLINVSGD AVVFVRESDL EVVSSQQPTT NCQSSCTEGE
VTT
Note: No experimental confirmation available.Curated
Show »Length:1,053
Mass (Da):116,305
<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:iF27416DC231838AA
Isoform 5 (identifier: Q86YS7-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
382-382: P → PAFVGIMGNTRSYKLLDWNSFNS
845-845: A → EHLESASSNSGIPAAQRDRCSSWIELIKLKAQTIRRGSIKTT
10 20 30 40 50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ
60 70 80 90 100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE
110 120 130 140 150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT
160 170 180 190 200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS
210 220 230 240 250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS
260 270 280 290 300
PAAFLPACNS PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV
310 320 330 340 350
SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQREFP FFTLTAFPPG
360 370 380 390 400
FLVHVGGVVS ARSVKLLDRI HNPAFVGIMG NTRSYKLLDW NSFNSDEPET
410 420 430 440 450
RDAWWAEIRQ EIKSHAKALG CHAVVGYSES TSICEEVCIL SASGTAAVLN
460 470 480 490 500
PRFLQDGTVE GCLEQRLEEN LPTRCGFCHI PYDELNMPFP AHLTYCYNCR
510 520 530 540 550
KQKVPDVLFT TIDLPTDATV IGKGCLIQAR LCRLKKKAQA EANATAISNL
560 570 580 590 600
LPFMEYEVHT QLMNKLKLKG MNALFGLRIQ ITVGENMLMG LASATGVYLA
610 620 630 640 650
ALPTPGGIQI AGKTPNDGSY EQHISHMQKK INDTIAKNKE LYEINPPEIS
660 670 680 690 700
EEIIGSPIPE PRQRSRLLRS QSESSDEVTE LDLSHGKKDA FVLEIDDTDA
710 720 730 740 750
MEDVHSLLTD VPPPSGFYSC NTEIMPGINN WTSEIQMFTS VRVIRLSSLN
760 770 780 790 800
LTNQALNKNF NDLCENLLKS LYFKLRSMIP CCLCHVNFTV SLPEDELIQV
810 820 830 840 850
TVTAVAITFD KNQALQTTKT PVEKSLQRAS TDNEELLQFP LELCSDSLPS
860 870 880 890 900
HPFPPAKEHL ESASSNSGIP AAQRDRCSSW IELIKLKAQT IRRGSIKTTM
910 920 930 940 950
TVEKASPVGD GNFRNRSAPP CANSTVGVVK MTPLSFIPGA KITKYLGIIN
960 970 980 990 1000
MFFIRETTSL REEGGVSGFL HAFIAEVFAM VRAHVAALGG NAVVSYIMKQ
1010 1020 1030 1040 1050
CVFMENPNKN QAQCLINVSG DAVVFVRESD LEVVSSQQPT TNCQSSCTEG
EVTT
Note: No experimental confirmation available.Curated
Show »Length:1,054
Mass (Da):116,468
<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:i2514DE8DDDBDB3A7
<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 BAA25454 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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 | 997 | E → G in BAG58665 (PubMed:14702039).Curated | 1 | ||
| Isoform 4 (identifier: Q86YS7-4) | |||||
| <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 | 895 | I → F in AAI43879 (PubMed:15489334).Curated | 1 | ||
| Isoform 5 (identifier: Q86YS7-5) | |||||
| <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 | 895 | S → P in BAG58665 (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 | AB011100 mRNA Translation: BAA25454.3 Different initiation. AY166851 mRNA Translation: AAO17290.1 AK295862 mRNA Translation: BAG58665.1 Frameshift. AK299353 mRNA Translation: BAG61349.1 AC053513 Genomic DNA No translation available. BC042498 mRNA Translation: AAH42498.2 BC053885 mRNA Translation: AAH53885.1 BC117143 mRNA Translation: AAI17144.1 BC143878 mRNA Translation: AAI43879.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31758.1 [Q86YS7-1] CCDS66337.1 [Q86YS7-3] CCDS66338.1 [Q86YS7-2] CCDS66339.1 [Q86YS7-5] CCDS66340.1 [Q86YS7-4] |
Protein sequence database of the Protein Information Resource More...PIRi | T00072 |
NCBI Reference Sequences More...RefSeqi | NP_001273102.1, NM_001286173.1 [Q86YS7-4] NP_001273103.1, NM_001286174.1 [Q86YS7-3] NP_001273104.1, NM_001286175.1 [Q86YS7-5] NP_001273105.1, NM_001286176.1 [Q86YS7-3] NP_001273106.1, NM_001286177.1 [Q86YS7-2] NP_055617.1, NM_014802.2 [Q86YS7-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.271014 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000333957; ENSP00000334229; ENSG00000111731 [Q86YS7-1] ENST00000396028; ENSP00000379345; ENSG00000111731 [Q86YS7-2] ENST00000446597; ENSP00000388756; ENSG00000111731 [Q86YS7-3] ENST00000536386; ENSP00000439392; ENSG00000111731 [Q86YS7-4] ENST00000542676; ENSP00000441951; ENSG00000111731 [Q86YS7-3] ENST00000545552; ENSP00000443204; ENSG00000111731 [Q86YS7-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9847 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9847 |
UCSC genome browser More...UCSCi | uc001rfq.5 human [Q86YS7-1] |
<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 | |
|---|---|---|---|---|---|
| Q86YS7 | C2 calcium dependent domain containing 5 | 1081 | |||
| UPI0004BD0503 | 1011 | ||||
| UPI00071961D9 | 1011 | ||||
| UPI00071A4C03 | 1011 | ||||
| UPI00071A4D2C | 1011 | ||||
| +90 | |||||
| Q86YS7-2 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI00080A2781 | 1064 | ||||
| +331 | |||||
| Q86YS7-3 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI00080A2781 | 1064 | ||||
| +331 | |||||
| Q86YS7-4 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI00080A2781 | 1064 | ||||
| +331 | |||||
| Q86YS7-5 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI00080A2781 | 1064 | ||||
| +331 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q86YS7 | C2 calcium dependent domain containing 5 | 1081 | |||
| UPI00071961D9 | 1011 | ||||
| UPI000981796D | 1011 | ||||
| UPI0004BD0503 | 1011 | ||||
| UPI00071A4C03 | 1011 | ||||
| +184 | |||||
| Q86YS7-2 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI0009442D1E | 1064 | ||||
| +1004 | |||||
| Q86YS7-3 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI0009442D1E | 1064 | ||||
| +1004 | |||||
| Q86YS7-4 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI0009442D1E | 1064 | ||||
| +1004 | |||||
| Q86YS7-5 | UPI000C7F4746 | 1069 | |||
| UPI000788374B | 1068 | ||||
| UPI00093ABE0E | 1067 | ||||
| UPI0004ED58C4 | 1067 | ||||
| UPI0009442D1E | 1064 | ||||
| +1004 | |||||
<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 | AB011100 mRNA Translation: BAA25454.3 Different initiation. AY166851 mRNA Translation: AAO17290.1 AK295862 mRNA Translation: BAG58665.1 Frameshift. AK299353 mRNA Translation: BAG61349.1 AC053513 Genomic DNA No translation available. BC042498 mRNA Translation: AAH42498.2 BC053885 mRNA Translation: AAH53885.1 BC117143 mRNA Translation: AAI17144.1 BC143878 mRNA Translation: AAI43879.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31758.1 [Q86YS7-1] CCDS66337.1 [Q86YS7-3] CCDS66338.1 [Q86YS7-2] CCDS66339.1 [Q86YS7-5] CCDS66340.1 [Q86YS7-4] |
Protein sequence database of the Protein Information Resource More...PIRi | T00072 |
NCBI Reference Sequences More...RefSeqi | NP_001273102.1, NM_001286173.1 [Q86YS7-4] NP_001273103.1, NM_001286174.1 [Q86YS7-3] NP_001273104.1, NM_001286175.1 [Q86YS7-5] NP_001273105.1, NM_001286176.1 [Q86YS7-3] NP_001273106.1, NM_001286177.1 [Q86YS7-2] NP_055617.1, NM_014802.2 [Q86YS7-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.271014 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q86YS7 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q86YS7 |
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 | 115182, 38 interactors |
Protein interaction database and analysis system More...IntActi | Q86YS7, 22 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000334229 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q86YS7 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q86YS7 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 74750574 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q86YS7 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q86YS7 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q86YS7 |
PeptideAtlas More...PeptideAtlasi | Q86YS7 |
PRoteomics IDEntifications database More...PRIDEi | Q86YS7 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 70464 70465 [Q86YS7-2] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000333957; ENSP00000334229; ENSG00000111731 [Q86YS7-1] ENST00000396028; ENSP00000379345; ENSG00000111731 [Q86YS7-2] ENST00000446597; ENSP00000388756; ENSG00000111731 [Q86YS7-3] ENST00000536386; ENSP00000439392; ENSG00000111731 [Q86YS7-4] ENST00000542676; ENSP00000441951; ENSG00000111731 [Q86YS7-3] ENST00000545552; ENSP00000443204; ENSG00000111731 [Q86YS7-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9847 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9847 |
UCSC genome browser More...UCSCi | uc001rfq.5 human [Q86YS7-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9847 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000111731.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | C2CD5 |
Human Gene Nomenclature Database More...HGNCi | HGNC:29062 C2CD5 |
Human Protein Atlas More...HPAi | HPA046194 |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q86YS7 |
Open Targets More...OpenTargetsi | ENSG00000111731 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA143485515 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1031 Eukaryota ENOG410XQDE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000000212 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000006746 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG081824 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q86YS7 |
Identification of Orthologs from Complete Genome Data More...OMAi | CANSTVG |
Database of Orthologous Groups More...OrthoDBi | EOG091G0FX6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q86YS7 |
TreeFam database of animal gene trees More...TreeFami | TF323431 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1445148 Translocation of GLUT4 to the plasma membrane |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | C2CD5 human |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9847 |
Protein Ontology More...PROi | PR:Q86YS7 |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000111731 |
CleanEx database of gene expression profiles More...CleanExi | HS_KIAA0528 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q86YS7 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q86YS7 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd08688 C2_KIAA0528-like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.150, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037785 C2_C2CD5 IPR000008 C2_dom IPR035892 C2_domain_sf IPR038983 C2CD5 |
The PANTHER Classification System More...PANTHERi | PTHR37412 PTHR37412, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00168 C2, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00239 C2, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50004 C2, 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 | C2CD5_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 | Q86YS7Primary (citable) accession number: Q86YS7 Secondary accession number(s): B4DJ03 , B4DRN7, B7ZLL0, F5H2A1, F5H5R1, O60280, Q17RY7, Q7Z619, Q86SU3 | |
| <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 25, 2006 |
| Last sequence update: | June 1, 2003 | |
| Last modified: | July 18, 2018 | |
| 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
Complete proteome, Reference proteomeDocuments
- Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM
