UniProtKB - P56945 (BCAR1_HUMAN)
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- BLAST>sp|P56945|BCAR1_HUMAN Breast cancer anti-estrogen resistance protein 1 OS=Homo sapiens OX=9606 GN=BCAR1 PE=1 SV=2 MNHLNVLAKALYDNVAESPDELSFRKGDIMTVLEQDTQGLDGWWLCSLHGRQGIVPGNRL KILVGMYDKKPAGPGPGPPATPAQPQPGLHAPAPPASQYTPMLPNTYQPQPDSVYLVPTP SKAQQGLYQVPGPSPQFQSPPAKQTSTFSKQTPHHPFPSPATDLYQVPPGPGGPAQDIYQ VPPSAGMGHDIYQVPPSMDTRSWEGTKPPAKVVVPTRVGQGYVYEAAQPEQDEYDIPRHL LAPGPQDIYDVPPVRGLLPSQYGQEVYDTPPMAVKGPNGRDPLLEVYDVPPSVEKGLPPS NHHAVYDVPPSVSKDVPDGPLLREETYDVPPAFAKAKPFDPARTPLVLAAPPPDSPPAED VYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGGVVDSGVYAVPPPAEREA PAEGKRLSASSTGSTRSSQSASSLEVAGPGREPLELEVAVEALARLQQGVSATVAHLLDL AGSAGATGSWRSPSEPQEPLVQDLQAAVAAVQSAVHELLEFARSAVGNAAHTSDRALHAK LSRQLQKMEDVHQTLVAHGQALDAGRGGSGATLEDLDRLVACSRAVPEDAKQLASFLHGN ASLLFRRTKATAPGPEGGGTLHPNPTDKTSSIQSRPLPSPPKFTSQDSPDGQYENSEGGW MEDYDYVHLQGKEEFEKTQKELLEKGSITRQGKSQLELQQLKQFERLEQEVSRPIDHDLA NWTPAQPLAPGRTGGLGPSDRQLLLFYLEQCEANLTTLTNAVDAFFTAVATNQPPKIFVA HSKFVILSAHKLVFIGDTLSRQAKAADVRSQVTHYSNLLCDLLRGIVATTKAAALQYPSP SAAQDMVERVKELGHSTQQFRRVLGQLAAA
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Protein
Breast cancer anti-estrogen resistance protein 1
Gene
BCAR1
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
Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.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.10"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX. - Ref.11"Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
Modzelewska K., Newman L.P., Desai R., Keely P.J.
J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- SH3 domain binding Source: UniProtKB-KW
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- actin filament organization 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
- antigen receptor-mediated signaling pathway 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
- B cell receptor signaling pathway 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
- cell adhesion Source: UniProtKB-KW
- cell chemotaxis Source: BHF-UCL <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
- cell division Source: UniProtKB <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
- cell migration 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
- cell proliferation 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
- cellular response to hepatocyte growth factor stimulus Source: BHF-UCL <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
- epidermal growth factor receptor signaling pathway Source: UniProtKB
- G-protein coupled receptor signaling pathway Source: UniProtKB
- hepatocyte growth factor receptor signaling pathway Source: BHF-UCL <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
- insulin receptor signaling pathway Source: UniProtKB
- integrin-mediated signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neurotrophin TRK receptor signaling pathway Source: UniProtKB
- platelet-derived growth factor receptor signaling pathway Source: UniProtKB
- positive regulation of cell migration 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
- positive regulation of endothelial cell migration Source: BHF-UCL <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
- regulation of apoptotic process Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of cell growth Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- T cell receptor signaling pathway Source: UniProtKB <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
- vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL <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
<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 | Cell adhesion |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-186763 Downstream signal transduction R-HSA-372708 p130Cas linkage to MAPK signaling for integrins R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P56945 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P56945 |
<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: Breast cancer anti-estrogen resistance protein 1Alternative name(s): CRK-associated substrate Cas scaffolding protein family member 1 p130cas |
| <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:BCAR1 Synonyms:CAS, CASS1, CRKAS |
| <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:ENSG00000050820.16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:971 BCAR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602941 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P56945 |
<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
Other locations
- focal adhesion 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.10"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX.
- Cytoplasm 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.10"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX.
Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation.By similarity- focal adhesion 1 Publication
Cytoskeleton
- actin cytoskeleton Source: Ensembl
Cytosol
- cytosol Source: Reactome
Other locations
- cytoplasm 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
- focal adhesion Source: BHF-UCL <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
- lamellipodium Source: Ensembl
- ruffle 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 junction, Cytoplasm<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
Organism-specific databases
DisGeNET More...DisGeNETi | 9564 |
Open Targets More...OpenTargetsi | ENSG00000050820 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25281 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BCAR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 288558806 |
<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_0000064854 | 1 – 870 | Breast cancer anti-estrogen resistance protein 1Add BLAST | 870 |
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 | 1 | N-acetylmethionine1 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 | 128 | Phosphotyrosine; by SRC1 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 | 134 | 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 | 139 | 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
<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 | 234 | 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 | 249 | Phosphotyrosine; by ABL1By 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 | 269 | 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 | 292 | 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 | 362 | 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 | 372 | 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 | 410 | 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 | 428 | 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 | 437 | 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 | 639 | 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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section 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
PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. SRC-family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin-mediated adhesion of cells to the extracellular matrix.4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX. - Ref.13"AND-34/BCAR3 regulates adhesion-dependent p130Cas serine phosphorylation and breast cancer cell growth pattern."
Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A., Cai D., Costello C.E., Lerner A.
Cell. Signal. 21:1423-1435(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, INTERACTION WITH BCAR3. - Ref.15"Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling."
Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F., Giancotti F.G.
J. Clin. Invest. 119:252-266(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1. - Ref.20"Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14."
Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C., Markowitz S.D., Polakiewicz R.D., Wang Z.
Oncogene 32:2087-2095(2013) [PubMed] [Europe PMC] [Abstract]Cited for: DEPHOSPHORYLATION AT TYR-128 BY PTPN14, PHOSPHORYLATION AT TYR-128 BY SRC.
Dephosphorylated by PTPN14 at Tyr-128.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P56945 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P56945 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P56945 |
PeptideAtlas More...PeptideAtlasi | P56945 |
PRoteomics IDEntifications database More...PRIDEi | P56945 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56960 56961 [P56945-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P56945 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P56945 |
<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
Widely expressed with an abundant expression in the testis. Low level of expression seen in the liver, thymus, and peripheral blood leukocytes. The protein has been detected in a B-cell line.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000050820 |
CleanEx database of gene expression profiles More...CleanExi | HS_BCAR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P56945 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P56945 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB000443 HPA042282 |
<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
Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1 and SH2D3C. Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part of a collagen-stimulated complex involved in cell migration made of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3 domains. Interacts with PTK2B/PYK2.8 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.8"Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas."
Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.
Nat. Cell Biol. 1:507-513(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CSPG4. - Ref.9"SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading."
Prasad N., Topping R.S., Decker S.J.
Mol. Cell. Biol. 21:1416-1428(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH INPPL1. - Ref.10"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX. - Ref.11"Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
Modzelewska K., Newman L.P., Desai R., Keely P.J.
J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK. - Ref.13"AND-34/BCAR3 regulates adhesion-dependent p130Cas serine phosphorylation and breast cancer cell growth pattern."
Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A., Cai D., Costello C.E., Lerner A.
Cell. Signal. 21:1423-1435(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, INTERACTION WITH BCAR3. - Ref.14"Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and regulates human glomerular mesangial cell adhesion and spreading."
Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A.
J. Cell. Physiol. 219:45-56(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTK2B/PYK2. - Ref.16"Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progression."
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L.
Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PEAK1. - Ref.22"NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling."
Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H., Pasquale E.B., Riedl S.J.
Nat. Struct. Mol. Biol. 18:1381-1387(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 645-870 IN COMPLEX WITH SH2D3C.
<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 |
|---|---|---|---|---|
| BCAR3 | O75815-1 | 3 | EBI-702093,EBI-15953103 | |
| CRK | P46108 | 5 | EBI-702093,EBI-886 | |
| FYN | P06241 | 3 | EBI-702093,EBI-515315 | |
| INPPL1 | O15357 | 2 | EBI-702093,EBI-1384248 | |
| IQGAP1 | P46940 | 4 | EBI-702093,EBI-297509 | |
| MMP14 | P50281 | 3 | EBI-702093,EBI-992788 | |
| PEAK1 | Q9H792 | 3 | EBI-702093,EBI-2609701 | |
| PTK2 | Q05397 | 2 | EBI-702093,EBI-702142 | |
| PTPN1 | P18031 | 5 | EBI-702093,EBI-968788 | |
| PTPN12 | Q05209 | 4 | EBI-702093,EBI-2266035 | |
| SH2D3C | Q8N5H7-2 | 8 | EBI-702093,EBI-15952996 | |
| SRC | P12931 | 3 | EBI-702093,EBI-621482 | |
| SRCIN1 | Q9C0H9 | 3 | EBI-702093,EBI-1393949 | |
| Srcin1 | Q9QWI6 | 3 | EBI-702093,EBI-775592 | From Mus musculus. |
| TNK2 | Q07912 | 5 | EBI-702093,EBI-603457 | |
| TNS | Q04205 | 2 | EBI-702093,EBI-2607590 | From Gallus gallus. |
| TNS3 | Q68CZ2 | 8 | EBI-702093,EBI-1220488 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- SH3 domain binding Source: UniProtKB-KW
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114934, 72 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P56945 |
Database of interacting proteins More...DIPi | DIP-33855N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P56945 |
Protein interaction database and analysis system More...IntActi | P56945, 261 interactors |
Molecular INTeraction database More...MINTi | P56945 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000391669 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 12 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 29 – 34 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 37 – 39 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 43 – 48 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 51 – 56 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 57 – 59 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 60 – 68 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 740 – 770 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 31 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 775 – 801 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 27 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 806 – 835 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 30 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 840 – 870 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 31 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P56945 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P56945 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P56945 |
<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 | 3 – 65 | SH3PROSITE-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 | 63 |
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 | 115 – 416 | Substrate for kinasesBy similarityAdd BLAST | 302 | |
| <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 | 746 – 796 | Divergent helix-loop-helix motifAdd BLAST | 51 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 635 – 643 | SH3-bindingSequence analysis | 9 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 74 – 87 | Pro-richAdd BLAST | 14 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 422 – 614 | Ser-richAdd BLAST | 193 |
<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
Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL1 SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9 (By similarity).By similarity
A serine-rich region promotes activation of the serum response element (SRE).
The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK11.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the CAS family.Curated
<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
SH3 domain, SH3-bindingPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IEDD Eukaryota ENOG410ZSUM LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00490000043324 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000261698 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004354 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P56945 |
KEGG Orthology (KO) More...KOi | K05726 |
Identification of Orthologs from Complete Genome Data More...OMAi | TVEHNQP |
Database of Orthologous Groups More...OrthoDBi | EOG091G0RVA |
Database for complete collections of gene phylogenies More...PhylomeDBi | P56945 |
TreeFam database of animal gene trees More...TreeFami | TF328782 |
Family and domain databases
Conserved Domains Database More...CDDi | cd12001 SH3_BCAR1, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.120.830, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR028848 BCAR1 IPR035745 BCAR1_SH3 IPR021901 CAS_C IPR037362 CAS_fam IPR014928 Serine_rich_dom IPR038319 Serine_rich_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain |
The PANTHER Classification System More...PANTHERi | PTHR10654 PTHR10654, 1 hit PTHR10654:SF15 PTHR10654:SF15, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF12026 DUF3513, 1 hit PF08824 Serine_rich, 1 hit PF00018 SH3_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00452 SH3DOMAIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00326 SH3, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50044 SSF50044, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50002 SH3, 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 (8)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 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: P56945-1) [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
MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG
60 70 80 90 100
RQGIVPGNRL KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT
110 120 130 140 150
PMLPNTYQPQ PDSVYLVPTP SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK
160 170 180 190 200
QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ VPPSAGMGHD IYQVPPSMDT
210 220 230 240 250
RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL LAPGPQDIYD
260 270 280 290 300
VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS
310 320 330 340 350
NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA
360 370 380 390 400
PPPDSPPAED VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA
410 420 430 440 450
DGGVVDSGVY AVPPPAEREA PAEGKRLSAS STGSTRSSQS ASSLEVAGPG
460 470 480 490 500
REPLELEVAV EALARLQQGV SATVAHLLDL AGSAGATGSW RSPSEPQEPL
510 520 530 540 550
VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK LSRQLQKMED
560 570 580 590 600
VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN
610 620 630 640 650
ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD
660 670 680 690 700
GQYENSEGGW MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ
710 720 730 740 750
LKQFERLEQE VSRPIDHDLA NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ
760 770 780 790 800
CEANLTTLTN AVDAFFTAVA TNQPPKIFVA HSKFVILSAH KLVFIGDTLS
810 820 830 840 850
RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP SAAQDMVERV
860 870
KELGHSTQQF RRVLGQLAAA
Length:870
Mass (Da):93,372
Last modified:February 9, 2010 - v2
<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:iB81EC3430049E795
Isoform 2 (identifier: P56945-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MNHL → MLTHRPQEAEQRGRTPGPSFEW
10 20 30 40 50
MLTHRPQEAE QRGRTPGPSF EWNVLAKALY DNVAESPDEL SFRKGDIMTV
60 70 80 90 100
LEQDTQGLDG WWLCSLHGRQ GIVPGNRLKI LVGMYDKKPA GPGPGPPATP
110 120 130 140 150
AQPQPGLHAP APPASQYTPM LPNTYQPQPD SVYLVPTPSK AQQGLYQVPG
160 170 180 190 200
PSPQFQSPPA KQTSTFSKQT PHHPFPSPAT DLYQVPPGPG GPAQDIYQVP
210 220 230 240 250
PSAGMGHDIY QVPPSMDTRS WEGTKPPAKV VVPTRVGQGY VYEAAQPEQD
260 270 280 290 300
EYDIPRHLLA PGPQDIYDVP PVRGLLPSQY GQEVYDTPPM AVKGPNGRDP
310 320 330 340 350
LLEVYDVPPS VEKGLPPSNH HAVYDVPPSV SKDVPDGPLL REETYDVPPA
360 370 380 390 400
FAKAKPFDPA RTPLVLAAPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG
410 420 430 440 450
PGTLYDVPRE RVLPPEVADG GVVDSGVYAV PPPAEREAPA EGKRLSASST
460 470 480 490 500
GSTRSSQSAS SLEVAGPGRE PLELEVAVEA LARLQQGVSA TVAHLLDLAG
510 520 530 540 550
SAGATGSWRS PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA RSAVGNAAHT
560 570 580 590 600
SDRALHAKLS RQLQKMEDVH QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC
610 620 630 640 650
SRAVPEDAKQ LASFLHGNAS LLFRRTKATA PGPEGGGTLH PNPTDKTSSI
660 670 680 690 700
QSRPLPSPPK FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL
710 720 730 740 750
LEKGSITRQG KSQLELQQLK QFERLEQEVS RPIDHDLANW TPAQPLAPGR
760 770 780 790 800
TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV DAFFTAVATN QPPKIFVAHS
810 820 830 840 850
KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCDL LRGIVATTKA
860 870 880
AALQYPSPSA AQDMVERVKE LGHSTQQFRR VLGQLAAA
Note: No experimental confirmation available.
Show »Length:888
Mass (Da):95,469
<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:i4CA6EC5C8EFE3DA6
Isoform 3 (identifier: P56945-3) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
304-304: A → AVSKCQGNARARLRLWGVW
10 20 30 40 50
MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG
60 70 80 90 100
RQGIVPGNRL KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT
110 120 130 140 150
PMLPNTYQPQ PDSVYLVPTP SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK
160 170 180 190 200
QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ VPPSAGMGHD IYQVPPSMDT
210 220 230 240 250
RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL LAPGPQDIYD
260 270 280 290 300
VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS
310 320 330 340 350
NHHAVSKCQG NARARLRLWG VWVYDVPPSV SKDVPDGPLL REETYDVPPA
360 370 380 390 400
FAKAKPFDPA RTPLVLAAPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG
410 420 430 440 450
PGTLYDVPRE RVLPPEVADG GVVDSGVYAV PPPAEREAPA EGKRLSASST
460 470 480 490 500
GSTRSSQSAS SLEVAGPGRE PLELEVAVEA LARLQQGVSA TVAHLLDLAG
510 520 530 540 550
SAGATGSWRS PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA RSAVGNAAHT
560 570 580 590 600
SDRALHAKLS RQLQKMEDVH QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC
610 620 630 640 650
SRAVPEDAKQ LASFLHGNAS LLFRRTKATA PGPEGGGTLH PNPTDKTSSI
660 670 680 690 700
QSRPLPSPPK FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL
710 720 730 740 750
LEKGSITRQG KSQLELQQLK QFERLEQEVS RPIDHDLANW TPAQPLAPGR
760 770 780 790 800
TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV DAFFTAVATN QPPKIFVAHS
810 820 830 840 850
KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCDL LRGIVATTKA
860 870 880
AALQYPSPSA AQDMVERVKE LGHSTQQFRR VLGQLAAA
Length:888
Mass (Da):95,454
<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:iFF81642D11EB93AC
Isoform 4 (identifier: P56945-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MNHL → MQGK
64-211: Missing.
10 20 30 40 50
MQGKNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG
60 70 80 90 100
RQGIVPGNRL KILVVVPTRV GQGYVYEAAQ PEQDEYDIPR HLLAPGPQDI
110 120 130 140 150
YDVPPVRGLL PSQYGQEVYD TPPMAVKGPN GRDPLLEVYD VPPSVEKGLP
160 170 180 190 200
PSNHHAVYDV PPSVSKDVPD GPLLREETYD VPPAFAKAKP FDPARTPLVL
210 220 230 240 250
AAPPPDSPPA EDVYDVPPPA PDLYDVPPGL RRPGPGTLYD VPRERVLPPE
260 270 280 290 300
VADGGVVDSG VYAVPPPAER EAPAEGKRLS ASSTGSTRSS QSASSLEVAG
310 320 330 340 350
PGREPLELEV AVEALARLQQ GVSATVAHLL DLAGSAGATG SWRSPSEPQE
360 370 380 390 400
PLVQDLQAAV AAVQSAVHEL LEFARSAVGN AAHTSDRALH AKLSRQLQKM
410 420 430 440 450
EDVHQTLVAH GQALDAGRGG SGATLEDLDR LVACSRAVPE DAKQLASFLH
460 470 480 490 500
GNASLLFRRT KATAPGPEGG GTLHPNPTDK TSSIQSRPLP SPPKFTSQDS
510 520 530 540 550
PDGQYENSEG GWMEDYDYVH LQGKEEFEKT QKELLEKGSI TRQGKSQLEL
560 570 580 590 600
QQLKQFERLE QEVSRPIDHD LANWTPAQPL APGRTGGLGP SDRQLLLFYL
610 620 630 640 650
EQCEANLTTL TNAVDAFFTA VATNQPPKIF VAHSKFVILS AHKLVFIGDT
660 670 680 690 700
LSRQAKAADV RSQVTHYSNL LCDLLRGIVA TTKAAALQYP SPSAAQDMVE
710 720
RVKELGHSTQ QFRRVLGQLA AA
Note: No experimental confirmation available.
Show »Length:722
Mass (Da):77,731
<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:i2537ED6C3BEBE512
Isoform 5 (identifier: P56945-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MNHL → ME
10 20 30 40 50
MENVLAKALY DNVAESPDEL SFRKGDIMTV LEQDTQGLDG WWLCSLHGRQ
60 70 80 90 100
GIVPGNRLKI LVGMYDKKPA GPGPGPPATP AQPQPGLHAP APPASQYTPM
110 120 130 140 150
LPNTYQPQPD SVYLVPTPSK AQQGLYQVPG PSPQFQSPPA KQTSTFSKQT
160 170 180 190 200
PHHPFPSPAT DLYQVPPGPG GPAQDIYQVP PSAGMGHDIY QVPPSMDTRS
210 220 230 240 250
WEGTKPPAKV VVPTRVGQGY VYEAAQPEQD EYDIPRHLLA PGPQDIYDVP
260 270 280 290 300
PVRGLLPSQY GQEVYDTPPM AVKGPNGRDP LLEVYDVPPS VEKGLPPSNH
310 320 330 340 350
HAVYDVPPSV SKDVPDGPLL REETYDVPPA FAKAKPFDPA RTPLVLAAPP
360 370 380 390 400
PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG
410 420 430 440 450
GVVDSGVYAV PPPAEREAPA EGKRLSASST GSTRSSQSAS SLEVAGPGRE
460 470 480 490 500
PLELEVAVEA LARLQQGVSA TVAHLLDLAG SAGATGSWRS PSEPQEPLVQ
510 520 530 540 550
DLQAAVAAVQ SAVHELLEFA RSAVGNAAHT SDRALHAKLS RQLQKMEDVH
560 570 580 590 600
QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC SRAVPEDAKQ LASFLHGNAS
610 620 630 640 650
LLFRRTKATA PGPEGGGTLH PNPTDKTSSI QSRPLPSPPK FTSQDSPDGQ
660 670 680 690 700
YENSEGGWME DYDYVHLQGK EEFEKTQKEL LEKGSITRQG KSQLELQQLK
710 720 730 740 750
QFERLEQEVS RPIDHDLANW TPAQPLAPGR TGGLGPSDRQ LLLFYLEQCE
760 770 780 790 800
ANLTTLTNAV DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ
810 820 830 840 850
AKAADVRSQV THYSNLLCDL LRGIVATTKA AALQYPSPSA AQDMVERVKE
860
LGHSTQQFRR VLGQLAAA
Note: No experimental confirmation available.
Show »Length:868
Mass (Da):93,137
<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:iDB6B70B2AB1926CD
Isoform 6 (identifier: P56945-6) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MNHL → MPAKPFLSSVLLSWKVLDFSGPGPQGTGQPCSCGHWAEGQGGPPEPAGGP
10 20 30 40 50
MPAKPFLSSV LLSWKVLDFS GPGPQGTGQP CSCGHWAEGQ GGPPEPAGGP
60 70 80 90 100
NVLAKALYDN VAESPDELSF RKGDIMTVLE QDTQGLDGWW LCSLHGRQGI
110 120 130 140 150
VPGNRLKILV GMYDKKPAGP GPGPPATPAQ PQPGLHAPAP PASQYTPMLP
160 170 180 190 200
NTYQPQPDSV YLVPTPSKAQ QGLYQVPGPS PQFQSPPAKQ TSTFSKQTPH
210 220 230 240 250
HPFPSPATDL YQVPPGPGGP AQDIYQVPPS AGMGHDIYQV PPSMDTRSWE
260 270 280 290 300
GTKPPAKVVV PTRVGQGYVY EAAQPEQDEY DIPRHLLAPG PQDIYDVPPV
310 320 330 340 350
RGLLPSQYGQ EVYDTPPMAV KGPNGRDPLL EVYDVPPSVE KGLPPSNHHA
360 370 380 390 400
VYDVPPSVSK DVPDGPLLRE ETYDVPPAFA KAKPFDPART PLVLAAPPPD
410 420 430 440 450
SPPAEDVYDV PPPAPDLYDV PPGLRRPGPG TLYDVPRERV LPPEVADGGV
460 470 480 490 500
VDSGVYAVPP PAEREAPAEG KRLSASSTGS TRSSQSASSL EVAGPGREPL
510 520 530 540 550
ELEVAVEALA RLQQGVSATV AHLLDLAGSA GATGSWRSPS EPQEPLVQDL
560 570 580 590 600
QAAVAAVQSA VHELLEFARS AVGNAAHTSD RALHAKLSRQ LQKMEDVHQT
610 620 630 640 650
LVAHGQALDA GRGGSGATLE DLDRLVACSR AVPEDAKQLA SFLHGNASLL
660 670 680 690 700
FRRTKATAPG PEGGGTLHPN PTDKTSSIQS RPLPSPPKFT SQDSPDGQYE
710 720 730 740 750
NSEGGWMEDY DYVHLQGKEE FEKTQKELLE KGSITRQGKS QLELQQLKQF
760 770 780 790 800
ERLEQEVSRP IDHDLANWTP AQPLAPGRTG GLGPSDRQLL LFYLEQCEAN
810 820 830 840 850
LTTLTNAVDA FFTAVATNQP PKIFVAHSKF VILSAHKLVF IGDTLSRQAK
860 870 880 890 900
AADVRSQVTH YSNLLCDLLR GIVATTKAAA LQYPSPSAAQ DMVERVKELG
910
HSTQQFRRVL GQLAAA
Note: No experimental confirmation available.
Show »Length:916
Mass (Da):97,877
<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:i3A5FDEB4BA15527B
Isoform 7 (identifier: P56945-7) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MNHL → MHCPGEAPLAAPRPTPKDPCLR
10 20 30 40 50
MHCPGEAPLA APRPTPKDPC LRNVLAKALY DNVAESPDEL SFRKGDIMTV
60 70 80 90 100
LEQDTQGLDG WWLCSLHGRQ GIVPGNRLKI LVGMYDKKPA GPGPGPPATP
110 120 130 140 150
AQPQPGLHAP APPASQYTPM LPNTYQPQPD SVYLVPTPSK AQQGLYQVPG
160 170 180 190 200
PSPQFQSPPA KQTSTFSKQT PHHPFPSPAT DLYQVPPGPG GPAQDIYQVP
210 220 230 240 250
PSAGMGHDIY QVPPSMDTRS WEGTKPPAKV VVPTRVGQGY VYEAAQPEQD
260 270 280 290 300
EYDIPRHLLA PGPQDIYDVP PVRGLLPSQY GQEVYDTPPM AVKGPNGRDP
310 320 330 340 350
LLEVYDVPPS VEKGLPPSNH HAVYDVPPSV SKDVPDGPLL REETYDVPPA
360 370 380 390 400
FAKAKPFDPA RTPLVLAAPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG
410 420 430 440 450
PGTLYDVPRE RVLPPEVADG GVVDSGVYAV PPPAEREAPA EGKRLSASST
460 470 480 490 500
GSTRSSQSAS SLEVAGPGRE PLELEVAVEA LARLQQGVSA TVAHLLDLAG
510 520 530 540 550
SAGATGSWRS PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA RSAVGNAAHT
560 570 580 590 600
SDRALHAKLS RQLQKMEDVH QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC
610 620 630 640 650
SRAVPEDAKQ LASFLHGNAS LLFRRTKATA PGPEGGGTLH PNPTDKTSSI
660 670 680 690 700
QSRPLPSPPK FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL
710 720 730 740 750
LEKGSITRQG KSQLELQQLK QFERLEQEVS RPIDHDLANW TPAQPLAPGR
760 770 780 790 800
TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV DAFFTAVATN QPPKIFVAHS
810 820 830 840 850
KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCDL LRGIVATTKA
860 870 880
AALQYPSPSA AQDMVERVKE LGHSTQQFRR VLGQLAAA
Note: No experimental confirmation available.
Show »Length:888
Mass (Da):95,216
<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:iCD3BA8494536FC76
Isoform 8 (identifier: P56945-8) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MNHL → MSVP
10 20 30 40 50
MSVPNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG
60 70 80 90 100
RQGIVPGNRL KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT
110 120 130 140 150
PMLPNTYQPQ PDSVYLVPTP SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK
160 170 180 190 200
QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ VPPSAGMGHD IYQVPPSMDT
210 220 230 240 250
RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL LAPGPQDIYD
260 270 280 290 300
VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS
310 320 330 340 350
NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA
360 370 380 390 400
PPPDSPPAED VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA
410 420 430 440 450
DGGVVDSGVY AVPPPAEREA PAEGKRLSAS STGSTRSSQS ASSLEVAGPG
460 470 480 490 500
REPLELEVAV EALARLQQGV SATVAHLLDL AGSAGATGSW RSPSEPQEPL
510 520 530 540 550
VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK LSRQLQKMED
560 570 580 590 600
VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN
610 620 630 640 650
ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD
660 670 680 690 700
GQYENSEGGW MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ
710 720 730 740 750
LKQFERLEQE VSRPIDHDLA NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ
760 770 780 790 800
CEANLTTLTN AVDAFFTAVA TNQPPKIFVA HSKFVILSAH KLVFIGDTLS
810 820 830 840 850
RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP SAAQDMVERV
860 870
KELGHSTQQF RRVLGQLAAA
Note: No experimental confirmation available.
Show »Length:870
Mass (Da):93,291
<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:i2262F3718326A675
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 | 63 | L → S in BAB55230 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 236 | I → T in AAF27527 (Ref. 2) 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 | 254 | V → I in BAG54099 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 349 | A → G in AAF27527 (Ref. 2) 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 | 363 | D → Y in AAF27527 (Ref. 2) 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 | 385 | T → A in AAS48631 (Ref. 4) 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 | 428 | S → P in BAB55230 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 471 | S → G in BAB55230 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 600 | N → S in AAS48631 (Ref. 4) 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 | 700 | Q → R in BAH13763 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 714 | P → L in BAG54099 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 740 | D → G in AAS48631 (Ref. 4) Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058970 | 76 | P → S4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_035798 | 407 | S → T in a breast cancer sample; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057820 | 491 | R → L. Corresponds to variant dbSNP:rs16957558Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057821 | 558 | H → R. Corresponds to variant dbSNP:rs16957552Ensembl. | 1 |
Alternative sequence
Sequence databases
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000162330; ENSP00000162330; ENSG00000050820 [P56945-1] ENST00000393420; ENSP00000377072; ENSG00000050820 [P56945-3] ENST00000393422; ENSP00000377074; ENSG00000050820 [P56945-7] ENST00000418647; ENSP00000391669; ENSG00000050820 [P56945-6] ENST00000420641; ENSP00000392708; ENSG00000050820 [P56945-2] ENST00000535626; ENSP00000440370; ENSG00000050820 [P56945-4] ENST00000538440; ENSP00000443841; ENSG00000050820 [P56945-8] ENST00000542031; ENSP00000440415; ENSG00000050820 [P56945-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9564 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9564 |
UCSC genome browser More...UCSCi | uc002fdv.4 human [P56945-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P56945 | UPI000642D54F | 1001 | |||
| BCAR1, Cas family scaffolding protein | 920 | ||||
| BCAR1 isoform 5 | 916 | ||||
| BCAR1, Cas family scaffolding protein | 916 | ||||
| UPI0005F4D9AC | 907 | ||||
| +500 | |||||
| P56945-4 | breast cancer anti-estrogen resistance protein 1 | 730 | |||
| BCAR1, Cas family scaffolding protein | 722 | ||||
| Breast cancer anti-estrogen resistance protein 1 | 722 | ||||
| BCAR1, Cas family scaffolding protein | 722 | ||||
| BCAR1 isoform 11 | 722 | ||||
| +23 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1WYX | X-ray | 1.14 | A/B | 3-71 | [»] | |
| 3T6G | X-ray | 2.50 | B/D | 645-870 | [»] | |
| 5O2M | NMR | - | A | 4-73 | [»] | |
| 5O2P | NMR | - | A | 4-73 | [»] | |
| 5O2Q | NMR | - | A | 4-73 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P56945 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P56945 | |||||
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 | 114934, 72 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P56945 |
Database of interacting proteins More...DIPi | DIP-33855N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P56945 |
Protein interaction database and analysis system More...IntActi | P56945, 261 interactors |
Molecular INTeraction database More...MINTi | P56945 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000391669 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P56945 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P56945 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BCAR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 288558806 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P56945 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P56945 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P56945 |
PeptideAtlas More...PeptideAtlasi | P56945 |
PRoteomics IDEntifications database More...PRIDEi | P56945 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56960 56961 [P56945-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 9564 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000162330; ENSP00000162330; ENSG00000050820 [P56945-1] ENST00000393420; ENSP00000377072; ENSG00000050820 [P56945-3] ENST00000393422; ENSP00000377074; ENSG00000050820 [P56945-7] ENST00000418647; ENSP00000391669; ENSG00000050820 [P56945-6] ENST00000420641; ENSP00000392708; ENSG00000050820 [P56945-2] ENST00000535626; ENSP00000440370; ENSG00000050820 [P56945-4] ENST00000538440; ENSP00000443841; ENSG00000050820 [P56945-8] ENST00000542031; ENSP00000440415; ENSG00000050820 [P56945-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9564 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9564 |
UCSC genome browser More...UCSCi | uc002fdv.4 human [P56945-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9564 |
DisGeNET More...DisGeNETi | 9564 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000050820.16 |
GeneCards: human genes, protein and diseases More...GeneCardsi | BCAR1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0173293 |
Human Gene Nomenclature Database More...HGNCi | HGNC:971 BCAR1 |
Human Protein Atlas More...HPAi | CAB000443 HPA042282 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602941 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P56945 |
Open Targets More...OpenTargetsi | ENSG00000050820 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25281 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IEDD Eukaryota ENOG410ZSUM LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00490000043324 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000261698 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004354 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P56945 |
KEGG Orthology (KO) More...KOi | K05726 |
Identification of Orthologs from Complete Genome Data More...OMAi | TVEHNQP |
Database of Orthologous Groups More...OrthoDBi | EOG091G0RVA |
Database for complete collections of gene phylogenies More...PhylomeDBi | P56945 |
TreeFam database of animal gene trees More...TreeFami | TF328782 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-186763 Downstream signal transduction R-HSA-372708 p130Cas linkage to MAPK signaling for integrins R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P56945 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P56945 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | BCAR1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P56945 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | BCAR1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9564 |
Protein Ontology More...PROi | PR:P56945 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000050820 |
CleanEx database of gene expression profiles More...CleanExi | HS_BCAR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P56945 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P56945 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd12001 SH3_BCAR1, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.120.830, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR028848 BCAR1 IPR035745 BCAR1_SH3 IPR021901 CAS_C IPR037362 CAS_fam IPR014928 Serine_rich_dom IPR038319 Serine_rich_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain |
The PANTHER Classification System More...PANTHERi | PTHR10654 PTHR10654, 1 hit PTHR10654:SF15 PTHR10654:SF15, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF12026 DUF3513, 1 hit PF08824 Serine_rich, 1 hit PF00018 SH3_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00452 SH3DOMAIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00326 SH3, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50044 SSF50044, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50002 SH3, 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 | BCAR1_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 | P56945Primary (citable) accession number: P56945 Secondary accession number(s): B3KWD7 , B4DEV4, B4DGB5, B4DIW5, B7Z7X7, E9PCL5, E9PCV2, F5GXA2, F5GXV6, F5H7Z0, F8WA69, Q6QEF7 | |
| <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: | May 30, 2000 |
| Last sequence update: | February 9, 2010 | |
| Last modified: | July 18, 2018 | |
| This is version 184 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
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
