UniProtKB - Q9NWQ8 (PHAG1_HUMAN)
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- BLAST>sp|Q9NWQ8|PHAG1_HUMAN Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 OS=Homo sapiens OX=9606 GN=PAG1 PE=1 SV=2 MGPAGSLLGSGQMQITLWGSLAAVAIFFVITFLIFLCSSCDREKKPRQHSGDHENLMNVP SDKEMFSRSVTSLATDAPASSEQNGALTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQD STGKPKCHQSRELPRIPPESAVDTMLTARSVDGDQGLGMEGPYEVLKDSSSQENMVEDCL YETVKEIKEVAAAAHLEKGHSGKAKSTSASKELPGPQTEGKAEFAEYASVDRNKKCRQSV NVESILGNSCDPEEEAPPPVPVKLLDENENLQEKEGGEAEESATDTTSETNKRFSSLSYK SREEDPTLTEEEISAMYSSVNKPGQLVNKSGQSLTVPESTYTSIQGDPQRSPSSCNDLYA TVKDFEKTPNSTLPPAGRPSEEPEPDYEAIQTLNREEEKATLGTNGHHGLVPKENDYESI SDLQQGRDITRL
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Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
PAG1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION.
<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
- SH2 domain binding Source: HGNC <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
- SH3/SH2 adaptor activity Source: HGNC <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- transmembrane receptor protein tyrosine kinase adaptor activity Source: GO_Central
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- adaptive immune response Source: UniProtKB-KW
- intracellular signal transduction Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of T cell activation Source: GO_Central
- regulation of T cell activation Source: ProtInc <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
- signal transduction Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- T cell receptor signaling pathway Source: Reactome
- transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
<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 | Adaptive immunity, Immunity |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-180292 GAB1 signalosome R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q9NWQ8 |
<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: Phosphoprotein associated with glycosphingolipid-enriched microdomains 1Alternative name(s): Csk-binding protein Transmembrane adapter protein PAG Transmembrane phosphoprotein Cbp |
| <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:PAG1 Synonyms:CBP, PAG |
| <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:ENSG00000076641.4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30043 PAG1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605767 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NWQ8 |
<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 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION. - Ref.8"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts."
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C.
Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION. - Ref.8"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts."
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C.
Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, SUBCELLULAR LOCATION.
Note: Present in lipid rafts.- Cell membrane 2 Publications
Plasma Membrane
- integral component of plasma membrane Source: GO_Central
- plasma membrane Source: HGNC <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
- intracellular Source: GOC
- membrane raft Source: HGNC <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
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 – 16 | ExtracellularSequence analysisAdd BLAST | 16 | |
| <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 | 17 – 37 | Helical; Signal-anchor for type III membrane proteinSequence 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 | 38 – 432 | CytoplasmicSequence analysisAdd BLAST | 395 |
<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, 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 | 105 | Y → F: No effect on interaction with FYN or CSK. 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 | 163 | Y → F: No effect on interaction with FYN or CSK. 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 | 181 | Y → F: No effect on interaction with FYN or CSK. 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 | 227 | Y → F: No effect on interaction with FYN or CSK. 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 | 299 | Y → F: No effect on interaction with FYN or CSK. 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 | 317 | Y → F: No effect on interaction with FYN. Abolishes interaction with CSK. 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 | 341 | Y → F: No effect on interaction with FYN or CSK. 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 | 359 | Y → F: No effect on interaction with FYN or CSK. 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 | 387 | Y → F: No effect on interaction with FYN or CSK. 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 | 417 | Y → F: No effect on interaction with FYN or CSK. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 55824 |
Open Targets More...OpenTargetsi | ENSG00000076641 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142671201 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PAG1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 84029384 |
<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_0000083338 | 1 – 432 | Phosphoprotein associated with glycosphingolipid-enriched microdomains 1Add BLAST | 432 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 37 | S-palmitoyl cysteine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 40 | S-palmitoyl cysteine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘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 | 50 | 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 | 61 | 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 | 105 | Phosphotyrosine; by LYNBy 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 | 163 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 181 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 227 | PhosphotyrosineCombined 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 | 229 | 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 | 317 | Phosphotyrosine; by FYN and LYNCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 354 | 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 | 359 | PhosphotyrosineCombined 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 | 380 | 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 | 387 | PhosphotyrosineCombined 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 | 417 | PhosphotyrosineCombined 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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION. - Ref.8"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts."
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C.
Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, SUBCELLULAR LOCATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Lipoprotein, Palmitate, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NWQ8 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NWQ8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NWQ8 |
PeptideAtlas More...PeptideAtlasi | Q9NWQ8 |
PRoteomics IDEntifications database More...PRIDEi | Q9NWQ8 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 82961 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q9NWQ8 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NWQ8 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NWQ8 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9NWQ8 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION. - Ref.7"Transmembrane adaptor molecules: a new category of lymphoid-cell markers."
Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T., Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M., Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.
Blood 107:213-221(2006) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000076641 |
CleanEx database of gene expression profiles More...CleanExi | HS_PAG1 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NWQ8 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA001632 HPA066527 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, FUNCTION. - Ref.5"Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton."
Brdickova N., Brdicka T., Andera L., Spicka J., Angelisova P., Milgram S.L., Horejsi V.
FEBS Lett. 507:133-136(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SLC9A3R1. - Ref.8"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts."
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C.
Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, SUBCELLULAR LOCATION.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CSK | P41240 | 3 | EBI-2828115,EBI-1380630 | |
| FYN | P06241 | 5 | EBI-2828115,EBI-515315 | |
| LYN | P07948 | 16 | EBI-2828115,EBI-79452 | |
| RACK1 | P63244 | 2 | EBI-2828115,EBI-296739 | |
| SLC9A3R1 | O14745 | 2 | EBI-2828115,EBI-349787 |
<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
- SH2 domain binding Source: HGNC <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
- SH3/SH2 adaptor activity Source: HGNC <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- transmembrane receptor protein tyrosine kinase adaptor activity Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 120931, 42 interactors |
Protein interaction database and analysis system More...IntActi | Q9NWQ8, 12 interactors |
Molecular INTeraction database More...MINTi | Q9NWQ8 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000220597 |
<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 | Q9NWQ8 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NWQ8 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 317 – 320 | Interaction with CSK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 4 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 430 – 432 | Interaction with SLC9A3R11 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
| 3 |
<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
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IFZ3 Eukaryota ENOG4111TW0 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000002061 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000290651 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG055052 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NWQ8 |
Identification of Orthologs from Complete Genome Data More...OMAi | KCHQSRE |
Database of Orthologous Groups More...OrthoDBi | EOG091G09DV |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NWQ8 |
TreeFam database of animal gene trees More...TreeFami | TF336170 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR032748 PAG |
The PANTHER Classification System More...PANTHERi | PTHR16322 PTHR16322, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF15347 PAG, 1 hit |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD340439 PD340439, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
10 20 30 40 50
MGPAGSLLGS GQMQITLWGS LAAVAIFFVI TFLIFLCSSC DREKKPRQHS
60 70 80 90 100
GDHENLMNVP SDKEMFSRSV TSLATDAPAS SEQNGALTNG DILSEDSTLT
110 120 130 140 150
CMQHYEEVQT SASDLLDSQD STGKPKCHQS RELPRIPPES AVDTMLTARS
160 170 180 190 200
VDGDQGLGME GPYEVLKDSS SQENMVEDCL YETVKEIKEV AAAAHLEKGH
210 220 230 240 250
SGKAKSTSAS KELPGPQTEG KAEFAEYASV DRNKKCRQSV NVESILGNSC
260 270 280 290 300
DPEEEAPPPV PVKLLDENEN LQEKEGGEAE ESATDTTSET NKRFSSLSYK
310 320 330 340 350
SREEDPTLTE EEISAMYSSV NKPGQLVNKS GQSLTVPEST YTSIQGDPQR
360 370 380 390 400
SPSSCNDLYA TVKDFEKTPN STLPPAGRPS EEPEPDYEAI QTLNREEEKA
410 420 430
TLGTNGHHGL VPKENDYESI SDLQQGRDIT RL
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 | 4 | A → V in AAH90931 (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 | 36 | L → P in BAA91321 (PubMed:14702039).Curated | 1 |
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 | AF240634 mRNA Translation: AAF67343.1 AK000680 mRNA Translation: BAA91321.1 AK289818 mRNA Translation: BAF82507.1 CH471068 Genomic DNA Translation: EAW87086.1 BC090931 mRNA Translation: AAH90931.1 BC112159 mRNA Translation: AAI12160.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6227.1 |
NCBI Reference Sequences More...RefSeqi | NP_060910.3, NM_018440.3 XP_016869129.1, XM_017013640.1 XP_016869130.1, XM_017013641.1 XP_016869131.1, XM_017013642.1 XP_016869132.1, XM_017013643.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.266175 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000220597; ENSP00000220597; ENSG00000076641 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55824 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55824 |
UCSC genome browser More...UCSCi | uc003ybz.4 human |
<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 | |
|---|---|---|---|---|---|
| Q9NWQ8 | phosphoprotein associated with glycosphingolipid-enriched microdomains 1 | 435 | |||
| PAG1 isoform 1 | 432 | ||||
| PAG1 isoform 1 | 432 | ||||
| Phosphoprotein membrane anchor with glycosphingolipid microdomains 1 | 432 | ||||
| Phosphoprotein membrane anchor with glycosphingolipid microdomains 1 | 432 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NWQ8 | phosphoprotein associated with glycosphingolipid-enriched microdomains 1 | 435 | |||
| Phosphoprotein membrane anchor with glycosphingolipid microdomains 1 | 432 | ||||
| PAG1 isoform 1 | 432 | ||||
| PAG1 isoform 1 | 432 | ||||
| Phosphoprotein membrane anchor with glycosphingolipid microdomains 1 | 432 | ||||
| +214 | |||||
<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 | AF240634 mRNA Translation: AAF67343.1 AK000680 mRNA Translation: BAA91321.1 AK289818 mRNA Translation: BAF82507.1 CH471068 Genomic DNA Translation: EAW87086.1 BC090931 mRNA Translation: AAH90931.1 BC112159 mRNA Translation: AAI12160.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6227.1 |
NCBI Reference Sequences More...RefSeqi | NP_060910.3, NM_018440.3 XP_016869129.1, XM_017013640.1 XP_016869130.1, XM_017013641.1 XP_016869131.1, XM_017013642.1 XP_016869132.1, XM_017013643.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.266175 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NWQ8 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NWQ8 |
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 | 120931, 42 interactors |
Protein interaction database and analysis system More...IntActi | Q9NWQ8, 12 interactors |
Molecular INTeraction database More...MINTi | Q9NWQ8 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000220597 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NWQ8 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NWQ8 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9NWQ8 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PAG1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 84029384 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NWQ8 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NWQ8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NWQ8 |
PeptideAtlas More...PeptideAtlasi | Q9NWQ8 |
PRoteomics IDEntifications database More...PRIDEi | Q9NWQ8 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 82961 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q9NWQ8 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 55824 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000220597; ENSP00000220597; ENSG00000076641 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55824 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55824 |
UCSC genome browser More...UCSCi | uc003ybz.4 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 55824 |
DisGeNET More...DisGeNETi | 55824 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000076641.4 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PAG1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30043 PAG1 |
Human Protein Atlas More...HPAi | HPA001632 HPA066527 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605767 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NWQ8 |
Open Targets More...OpenTargetsi | ENSG00000076641 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142671201 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IFZ3 Eukaryota ENOG4111TW0 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000002061 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000290651 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG055052 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NWQ8 |
Identification of Orthologs from Complete Genome Data More...OMAi | KCHQSRE |
Database of Orthologous Groups More...OrthoDBi | EOG091G09DV |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NWQ8 |
TreeFam database of animal gene trees More...TreeFami | TF336170 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-180292 GAB1 signalosome R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q9NWQ8 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PAG1 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | PAG1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 55824 |
Protein Ontology More...PROi | PR:Q9NWQ8 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000076641 |
CleanEx database of gene expression profiles More...CleanExi | HS_PAG1 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NWQ8 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR032748 PAG |
The PANTHER Classification System More...PANTHERi | PTHR16322 PTHR16322, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF15347 PAG, 1 hit |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD340439 PD340439, 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 | PHAG1_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 | Q9NWQ8Primary (citable) accession number: Q9NWQ8 Secondary accession number(s): A8K1A3 , Q2M1Z9, Q5BKU4, Q9NYK0 | |
| <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: | December 20, 2005 |
| Last sequence update: | December 20, 2005 | |
| Last modified: | July 18, 2018 | |
| This is version 134 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
