UniProtKB - Q05397 (FAK1_HUMAN)
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- BLAST>sp|Q05397|FAK1_HUMAN Focal adhesion kinase 1 OS=Homo sapiens OX=9606 GN=PTK2 PE=1 SV=2 MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGD ATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEW KYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSY WEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQ TIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFII RPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRE RIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDH PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESK RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFT SASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA YDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGY PSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQE IAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLS RGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNE GVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLA LRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQM LTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
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Focal adhesion kinase 1
PTK2
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION. - Ref.11"Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, INTERACTION WITH BMX. - Ref.12"Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples."
Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.
Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF SHC1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1 AND SRC, ROLE IN DISEASE. - Ref.15"Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway."
Xia H., Nho R.S., Kahm J., Kleidon J., Henke C.A.
J. Biol. Chem. 279:33024-33034(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN INTEGRIN SIGNALING; REGULATION OF APOPTOSIS; REGULATION OF CELL SHAPE AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND AKT1 SIGNALING PATHWAY. - Ref.16"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION AT TYR-407; TYR-397 AND TYR-576. - Ref.18"Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase."
Ezratty E.J., Partridge M.A., Gundersen G.G.
Nat. Cell Biol. 7:581-590(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FOCAL ADHESION DISASSEMBLY. - Ref.23"Therapeutic efficacy of a novel focal adhesion kinase inhibitor TAE226 in ovarian carcinoma."
Halder J., Lin Y.G., Merritt W.M., Spannuth W.A., Nick A.M., Honda T., Kamat A.A., Han L.Y., Kim T.J., Lu C., Tari A.M., Bornmann W., Fernandez A., Lopez-Berestein G., Sood A.K.
Cancer Res. 67:10976-10983(2007) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397 AND TYR-861. - Ref.24"Cellular characterization of a novel focal adhesion kinase inhibitor."
Slack-Davis J.K., Martin K.H., Tilghman R.W., Iwanicki M., Ung E.J., Autry C., Luzzio M.J., Cooper B., Kath J.C., Roberts W.G., Parsons J.T.
J. Biol. Chem. 282:14845-14852(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397. - Ref.25"Activation of FAK is necessary for the osteogenic differentiation of human mesenchymal stem cells on laminin-5."
Salasznyk R.M., Klees R.F., Boskey A., Plopper G.E.
J. Cell. Biochem. 100:499-514(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION. - Ref.26"Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo."
Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T., Jackson D., de Groot J., Yung W.K.
Mol. Cancer Ther. 6:1357-1367(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397. - Ref.27"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH LPXN. - Ref.28"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BMX. - Ref.29"A novel Cas family member, HEPL, regulates FAK and cell spreading."
Singh M.K., Dadke D., Nicolas E., Serebriiskii I.G., Apostolou S., Canutescu A., Egleston B.L., Golemis E.A.
Mol. Biol. Cell 19:1627-1636(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASS4. - Ref.30"Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation."
Lim S.T., Chen X.L., Lim Y., Hanson D.A., Vo T.T., Howerton K., Larocque N., Fisher S.J., Schlaepfer D.D., Ilic D.
Mol. Cell 29:9-22(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL SURVIVAL, SUBCELLULAR LOCATION. - Ref.36"Paxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion."
Sachdev S., Bu Y., Gelman I.H.
BMC Cancer 9:12-12(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN. - Ref.39"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: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF BCAR1, ROLE IN DISEASE. - Ref.42"Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models."
Sun H., Pisle S., Gardner E.R., Figg W.D.
Cancer Biol. Ther. 10:38-43(2010) [PubMed] [Europe PMC] [Abstract]Cited for: ROLE IN DISEASE, ENZYME REGULATION. - Ref.49"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism."
Plaza-Menacho I., Morandi A., Mologni L., Boender P., Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P., McDonald N.Q., Isacke C.M.
J. Biol. Chem. 286:17292-17302(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, PHOSPHORYLATION AT TYR-576 AND TYR-577. - Ref.54"Integrin-regulated FAK-Src signaling in normal and cancer cells."
Mitra S.K., Schlaepfer D.D.
Curr. Opin. Cell Biol. 18:516-523(2006) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW ON FUNCTION IN CELL MIGRATION; FOCAL ADHESION TURNOVER AND ACTIVATION OF SIGNALING PATHWAYS, ROLE IN DISEASE. - Ref.55"Focal adhesion kinase: an essential kinase in the regulation of cardiovascular functions."
Vadali K., Cai X., Schaller M.D.
IUBMB Life 59:709-716(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.56"FERM control of FAK function: implications for cancer therapy."
Lim S.T., Mikolon D., Stupack D.G., Schlaepfer D.D.
Cell Cycle 7:2306-2314(2008) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53 ACTIVITIES, ROLE IN DISEASE, ENZYME REGULATION. - Ref.58"Focal adhesion kinase and cancer."
Golubovskaya V.M., Kweh F.A., Cance W.G.
Histol. Histopathol. 24:503-510(2009) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW ON EXPRESSION IN CANCER, ROLE IN DISEASE. - Ref.62"Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions."
Schaller M.D.
J. Cell Sci. 123:1007-1013(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SIGNALING.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<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
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION. - Ref.11"Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, INTERACTION WITH BMX. - Ref.68"Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271."
Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C., Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L., Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N., Schmitt E. , LaGreca S., Jani J., Wessel M., Marr E., Griffor M., Vajdos F.
Cancer Res. 68:1935-1944(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION. - Ref.23"Therapeutic efficacy of a novel focal adhesion kinase inhibitor TAE226 in ovarian carcinoma."
Halder J., Lin Y.G., Merritt W.M., Spannuth W.A., Nick A.M., Honda T., Kamat A.A., Han L.Y., Kim T.J., Lu C., Tari A.M., Bornmann W., Fernandez A., Lopez-Berestein G., Sood A.K.
Cancer Res. 67:10976-10983(2007) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397 AND TYR-861. - Ref.24"Cellular characterization of a novel focal adhesion kinase inhibitor."
Slack-Davis J.K., Martin K.H., Tilghman R.W., Iwanicki M., Ung E.J., Autry C., Luzzio M.J., Cooper B., Kath J.C., Roberts W.G., Parsons J.T.
J. Biol. Chem. 282:14845-14852(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397. - Ref.26"Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo."
Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T., Jackson D., de Groot J., Yung W.K.
Mol. Cancer Ther. 6:1357-1367(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397. - Ref.42"Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models."
Sun H., Pisle S., Gardner E.R., Figg W.D.
Cancer Biol. Ther. 10:38-43(2010) [PubMed] [Europe PMC] [Abstract]Cited for: ROLE IN DISEASE, ENZYME REGULATION. - Ref.56"FERM control of FAK function: implications for cancer therapy."
Lim S.T., Mikolon D., Stupack D.G., Schlaepfer D.D.
Cell Cycle 7:2306-2314(2008) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53 ACTIVITIES, ROLE IN DISEASE, ENZYME REGULATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 454 | ATPPROSITE-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 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 ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 546 | Proton acceptorPROSITE-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 | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 428 – 434 | ATPPROSITE-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 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
| 7 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 500 – 502 | ATPPROSITE-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 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
| 3 |
<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
- actin binding 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
- ATP binding Source: UniProtKB-KW
- JUN kinase binding 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
- non-membrane spanning protein tyrosine kinase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein kinase activity Source: Reactome
- 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
- protein tyrosine kinase activity Source: ReactomeInferred from experimenti
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
- SH2 domain 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
- signaling receptor binding Source: GO_Central
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- angiogenesis 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
- axon guidance 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
- cell motility 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
- central nervous system neuron axonogenesis Source: Ensembl
- endothelial cell migration Source: Ensembl
- ephrin 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
- epidermal growth factor receptor signaling pathway Source: GO_Central
- establishment of cell polarity 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
- extracellular matrix organization Source: Ensembl
- Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
- growth hormone receptor signaling pathway 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
- heart morphogenesis 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
- innate immune response Source: GO_Central
- 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
- MAPK cascade Source: Reactome
- microtubule cytoskeleton organization Source: Ensembl
- negative regulation of anoikis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of apoptotic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of autophagy Source: Ensembl
- negative regulation of axonogenesis Source: Ensembl
- negative regulation of cell-cell 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
- negative regulation of organ growth Source: Ensembl
- negative regulation of synapse assembly Source: Ensembl
- netrin-activated signaling pathway 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
- neuron migration Source: Ensembl
- nuclear migration Source: Ensembl
- peptidyl-tyrosine autophosphorylation Source: GO_Central
- peptidyl-tyrosine phosphorylation 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
- placenta development 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
- positive regulation of cardiac muscle hypertrophy Source: Ensembl
- 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 cell proliferation Source: UniProtKB
- positive regulation of phosphatidylinositol 3-kinase activity 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
- positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein kinase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein kinase B signaling Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein phosphorylation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of ubiquitin-dependent protein catabolic process Source: UniProtKB
- protein autophosphorylation 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
- regulation of cell adhesion mediated by integrin 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
- regulation of cell proliferation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of cell shape Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of cytoskeleton organization 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 endothelial cell migration 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 epithelial cell migration Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- regulation of focal adhesion assembly Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- regulation of GTPase activity 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 osteoblast differentiation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of protein phosphorylation Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- regulation of substrate adhesion-dependent cell spreading Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- signal complex assembly Source: InterPro
- transforming growth factor beta 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
- vascular endothelial growth factor receptor signaling pathway Source: Reactome
- vasculogenesis Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Developmental protein, Kinase, Transferase, Tyrosine-protein kinase |
| Biological process | Angiogenesis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.2 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-111465 Apoptotic cleavage of cellular proteins R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-354192 Integrin alphaIIb beta3 signaling R-HSA-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins R-HSA-372708 p130Cas linkage to MAPK signaling for integrins R-HSA-375165 NCAM signaling for neurite out-growth R-HSA-391160 Signal regulatory protein family interactions R-HSA-3928662 EPHB-mediated forward signaling R-HSA-418885 DCC mediated attractive signaling R-HSA-418886 Netrin mediated repulsion signals R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs R-HSA-5673001 RAF/MAP kinase cascade R-HSA-8874081 MET activates PTK2 signaling |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q05397 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q05397 |
<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: Focal adhesion kinase 1 (EC:2.7.10.2)Short name: FADK 1 Alternative name(s): Focal adhesion kinase-related nonkinase Short name: FRNK Protein phosphatase 1 regulatory subunit 71 Short name: PPP1R71 Protein-tyrosine kinase 2 p125FAK pp125FAK |
| <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:PTK2 Synonyms:FAK, FAK1 |
| <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:ENSG00000169398.19 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9611 PTK2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600758 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q05397 |
<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
Nucleus
Cytoskeleton
- cytoskeleton
- centrosome By similarity
Plasma membrane
Other locations
Note: Constituent of focal adhesions. Detected at microtubules.
Cytoskeleton
- cytoskeleton 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
- microtubule organizing center Source: UniProtKB-SubCell
- stress fiber 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
Cytosol
- cytosol 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
Nucleus
- nucleus 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
Plasma Membrane
- apical plasma membrane Source: Ensembl
- extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
- plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cell cortex Source: UniProtKB-SubCell
- 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: 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
- lamellipodium Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 397 | Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 928 | V → G: Loss of interaction with TGFB1I1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1034 | L → S: Loss of interaction with TGFB1I1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 5747 |
Open Targets More...OpenTargetsi | ENSG00000169398 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33955 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2695 |
Drug and drug target database More...DrugBanki | DB07460 2-({5-CHLORO-2-[(2-METHOXY-4-MORPHOLIN-4-YLPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)-N-METHYLBENZAMIDE |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2180 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PTK2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 3183518 |
<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined 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
| |||
| <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_0000088077 | 2 – 1052 | Focal adhesion kinase 1Add BLAST | 1051 |
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 | 2 | N-acetylalanineCombined 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 | 5 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 13 | 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 | 29 | 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 | 54 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 152 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity | ||
| <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 | 397 | Phosphotyrosine; by autocatalysisCombined 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 | 407 | Phosphotyrosine2 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 ‘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 | 570 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 576 | Phosphotyrosine; by RET and SRC3 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 ‘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 | 577 | Phosphotyrosine; by RET and SRC3 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 ‘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 | 580 | 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 | 722 | 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 | 732 | Phosphoserine; by CDK5By 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 | 843 | 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 | 861 | Phosphotyrosine3 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 ‘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 | 887 | 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 | 910 | 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 | 914 | 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 | 925 | Phosphotyrosine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein."
Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.
Biochem. J. 369:407-416(2003) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, INTERACTION WITH FGR. - Ref.16"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION AT TYR-407; TYR-397 AND TYR-576. - Ref.23"Therapeutic efficacy of a novel focal adhesion kinase inhibitor TAE226 in ovarian carcinoma."
Halder J., Lin Y.G., Merritt W.M., Spannuth W.A., Nick A.M., Honda T., Kamat A.A., Han L.Y., Kim T.J., Lu C., Tari A.M., Bornmann W., Fernandez A., Lopez-Berestein G., Sood A.K.
Cancer Res. 67:10976-10983(2007) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397 AND TYR-861. - Ref.24"Cellular characterization of a novel focal adhesion kinase inhibitor."
Slack-Davis J.K., Martin K.H., Tilghman R.W., Iwanicki M., Ung E.J., Autry C., Luzzio M.J., Cooper B., Kath J.C., Roberts W.G., Parsons J.T.
J. Biol. Chem. 282:14845-14852(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397. - Ref.26"Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo."
Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T., Jackson D., de Groot J., Yung W.K.
Mol. Cancer Ther. 6:1357-1367(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397. - Ref.35"Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes."
Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G., Oh E.S., Buday L., Kim S.H., Lee J.W.
Biochim. Biophys. Acta 1793:781-791(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925, IDENTIFICATION IN A COMPLEX WITH CTTN AND FER. - Ref.49"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism."
Plaza-Menacho I., Morandi A., Mologni L., Boender P., Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P., McDonald N.Q., Isacke C.M.
J. Biol. Chem. 286:17292-17302(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
<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, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q05397 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q05397 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q05397 |
PeptideAtlas More...PeptideAtlasi | Q05397 |
PRoteomics IDEntifications database More...PRIDEi | Q05397 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 58320 58321 [Q05397-2] 58322 [Q05397-3] 58323 [Q05397-4] 58324 [Q05397-5] 58325 [Q05397-6] |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | Q05397 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q05397 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q05397 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | Q05397 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK."
Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A., Kanner S.B.
DNA Cell Biol. 12:823-830(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. - Ref.2"Expression of an N-terminally truncated form of human focal adhesion kinase in brain."
Andre E., Becker-Andre M.
Biochem. Biophys. Res. Commun. 190:140-147(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY. - Ref.7"A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
Lee S.-T., Strunk K.M., Spritz R.A.
Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, TISSUE SPECIFICITY. - Ref.44"Downregulation of FAK-related non-kinase mediates the migratory phenotype of human fibrotic lung fibroblasts."
Cai G.Q., Zheng A., Tang Q., White E.S., Chou C.F., Gladson C.L., Olman M.A., Ding Q.
Exp. Cell Res. 316:1600-1609(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORM 6), TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000169398 |
CleanEx database of gene expression profiles More...CleanExi | HS_PTK2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q05397 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q05397 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB004036 HPA001842 HPA029671 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions."
Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T.
J. Biol. Chem. 273:1003-1014(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TGFB1I1. - Ref.9"Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase."
Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.
J. Biol. Chem. 273:26516-26521(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TGFB1I1, MUTAGENESIS OF VAL-928 AND LEU-1034. - Ref.10"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION. - Ref.11"Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, INTERACTION WITH BMX. - Ref.12"Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples."
Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.
Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF SHC1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1 AND SRC, ROLE IN DISEASE. - Ref.13"Regulation of focal adhesion kinase by a novel protein inhibitor FIP200."
Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R., Guan J.L.
Mol. Biol. Cell 13:3178-3191(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RB1CC1. - Ref.14"Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein."
Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.
Biochem. J. 369:407-416(2003) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, INTERACTION WITH FGR. - Ref.17"Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53."
Golubovskaya V.M., Finch R., Cance W.G.
J. Biol. Chem. 280:25008-25021(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH P53/TP53, SUBCELLULAR LOCATION. - Ref.19"Vascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells."
Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.
Cancer Res. 66:1446-1454(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FLT4. - Ref.27"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH LPXN. - Ref.28"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BMX. - Ref.29"A novel Cas family member, HEPL, regulates FAK and cell spreading."
Singh M.K., Dadke D., Nicolas E., Serebriiskii I.G., Apostolou S., Canutescu A., Egleston B.L., Golemis E.A.
Mol. Biol. Cell 19:1627-1636(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASS4. - Ref.31"Regulation of estrogen rapid signaling through arginine methylation by PRMT1."
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.
Mol. Cell 31:212-221(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ESR1; PIK3R1 AND/OR PIK3R2 AND SRC. - Ref.35"Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes."
Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G., Oh E.S., Buday L., Kim S.H., Lee J.W.
Biochim. Biophys. Acta 1793:781-791(2009) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925, IDENTIFICATION IN A COMPLEX WITH CTTN AND FER. - Ref.37"STEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells."
Tamura T., Chiba J.
Int. J. Mol. Med. 24:599-604(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH STEAP4. - Ref.38"Functional consequences of interactions between FAK and epithelial membrane protein 2 (EMP2)."
Morales S.A., Mareninov S., Coulam P., Wadehra M., Goodglick L., Braun J., Gordon L.K.
Invest. Ophthalmol. Vis. Sci. 50:4949-4956(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EMP2. - Ref.40"EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EPHA1. - Ref.43"LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin."
Tanaka T., Moriwaki K., Murata S., Miyasaka M.
Cancer Sci. 101:363-368(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH LPXN. - Ref.45"ZF21 protein regulates cell adhesion and motility."
Nagano M., Hoshino D., Sakamoto T., Kawasaki N., Koshikawa N., Seiki M.
J. Biol. Chem. 285:21013-21022(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZFYVE21, DEPHOSPHORYLATION AT TYR-397. - Ref.46"CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer."
Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.
Nat. Immunol. 11:155-161(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD36. - Ref.49"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism."
Plaza-Menacho I., Morandi A., Mologni L., Boender P., Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P., McDonald N.Q., Isacke C.M.
J. Biol. Chem. 286:17292-17302(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, PHOSPHORYLATION AT TYR-576 AND TYR-577. - Ref.51"A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
Oncogene 33:1167-1180(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CIB1 ISOFORM 2. - Ref.64"MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MISP. - Ref.66"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 411-686 IN COMPLEX WITH ATP. - Ref.67"Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain."
Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., Arold S.T.
Structure 11:1207-1217(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 892-1052 IN COMPLEX WITH PXN, INTERACTION WITH PXN. - Ref.68"Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271."
Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C., Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L., Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N., Schmitt E. , LaGreca S., Jani J., Wessel M., Marr E., Griffor M., Vajdos F.
Cancer Res. 68:1935-1944(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION. - Ref.69"Structural basis for the interaction between focal adhesion kinase and CD4."
Garron M.L., Arthos J., Guichou J.F., McNally J., Cicala C., Arold S.T.
J. Mol. Biol. 375:1320-1328(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 891-1052 IN COMPLEX WITH CD4, SUBCELLULAR LOCATION, INTERACTION WITH CD4.
<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 |
|---|---|---|---|---|
| BCAR1 | P56945 | 2 | EBI-702142,EBI-702093 | |
| CCNA1 | P78396 | 2 | EBI-702142,EBI-375065 | |
| CRK | P46108 | 3 | EBI-702142,EBI-886 | |
| CRKL | P46109 | 2 | EBI-702142,EBI-910 | |
| EGFR | P00533 | 3 | EBI-702142,EBI-297353 | |
| EPHA2 | P29317 | 3 | EBI-702142,EBI-702104 | |
| ERBB2 | P04626 | 2 | EBI-702142,EBI-641062 | |
| FLT1 | P17948 | 2 | EBI-702142,EBI-1026718 | |
| GRB7 | Q14451 | 3 | EBI-702142,EBI-970191 | |
| HCK | P08631-2 | 2 | EBI-702142,EBI-9834454 | |
| ITGB4 | P16144 | 7 | EBI-702142,EBI-948678 | |
| LYN | P07948 | 2 | EBI-702142,EBI-79452 | |
| PIK3R3 | Q92569 | 3 | EBI-702142,EBI-79893 | |
| PTPN23 | Q9H3S7 | 4 | EBI-702142,EBI-724478 | |
| PTPN6 | P29350-3 | 3 | EBI-702142,EBI-7399369 | |
| PTRH2 | Q9Y3E5 | 2 | EBI-702142,EBI-1056751 | |
| PXN | P49023 | 15 | EBI-702142,EBI-702209 | |
| SH2D2A | Q9NP31 | 3 | EBI-702142,EBI-490630 | |
| SRC | P12931 | 8 | EBI-702142,EBI-621482 | |
| Src | P05480 | 5 | EBI-702142,EBI-298680 | From Mus musculus. |
| TGFB1I1 | O43294 | 2 | EBI-702142,EBI-1051449 | |
| Tgfb1i1 | Q62219 | 3 | EBI-702142,EBI-642844 | From Mus musculus. |
| TNS3 | Q68CZ2 | 3 | EBI-702142,EBI-1220488 | |
| TP53 | P04637 | 13 | EBI-702142,EBI-366083 |
<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
- actin binding 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
- JUN kinase binding 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
- 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
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
- SH2 domain 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
- signaling receptor binding Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111719, 126 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q05397 |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q05397 |
Protein interaction database and analysis system More...IntActi | Q05397, 70 interactors |
Molecular INTeraction database More...MINTi | Q05397 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000341189 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q05397 |
<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
| 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 | 35 – 40 | 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 | 49 – 51 | 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 | 53 – 58 | 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 | 64 – 73 | 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 | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 74 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 80 – 82 | 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 | 83 – 89 | 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 | 7 | |
| <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 | 95 – 98 | 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 | 4 | |
| <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 | 104 – 114 | 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 | 11 | |
| <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 | 117 – 119 | 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 | 120 – 126 | 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 | 7 | |
| <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 | 133 – 137 | 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 | 5 | |
| <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 | 141 – 158 | 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 | 18 | |
| <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 | 165 – 179 | 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 | 15 | |
| <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 | 185 – 187 | 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 | 188 – 190 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 191 – 194 | 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 | 4 | |
| <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 | 197 – 201 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 204 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 209 – 214 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 217 – 219 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 220 – 228 | 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 | 229 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 236 – 247 | 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 | 12 | |
| <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 | 248 – 250 | 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 | 256 – 262 | 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 | 7 | |
| <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 | 264 – 266 | 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 | 268 – 275 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 276 – 278 | 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 | 279 – 283 | 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 | 5 | |
| <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 | 290 – 294 | 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 | 5 | |
| <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 | 296 – 298 | 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 | 299 – 306 | 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 | 308 – 311 | 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 | 4 | |
| <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 | 314 – 320 | 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 | 7 | |
| <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 | 327 – 333 | 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 | 7 | |
| <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 | 334 – 351 | 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 | 18 | |
| <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 | 413 – 415 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 419 – 421 | 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 | 422 – 430 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 432 – 441 | 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 | 10 | |
| <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 | 444 – 446 | 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 | 448 – 455 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 457 – 460 | 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 | 4 | |
| <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 | 462 – 468 | 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 | 7 | |
| <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 | 470 – 476 | 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 | 7 | |
| <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 | 486 – 490 | 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 | 5 | |
| <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 | 492 – 494 | 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 | 496 – 500 | 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 | 5 | |
| <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 | 507 – 513 | 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 | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 514 – 517 | 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 | 4 | |
| <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 | 520 – 539 | 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 | 20 | |
| <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 | 549 – 551 | 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 | 552 – 556 | 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 | 5 | |
| <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 | 559 – 562 | 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 | 4 | |
| <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 | 565 – 568 | 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 | 4 | |
| <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 | 570 – 573 | 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 | 4 | |
| <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 | 574 – 576 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 586 – 588 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 591 – 596 | 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 | 601 – 616 | 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 | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 617 – 619 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 622 – 625 | 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 | 4 | |
| <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 | 628 – 630 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 631 – 636 | 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 | 649 – 658 | 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 | 10 | |
| <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 | 663 – 665 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 669 – 684 | 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 | 16 | |
| <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 | 685 – 687 | 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 | 915 – 917 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 923 – 942 | 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 | 20 | |
| <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 | 947 – 949 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 950 – 971 | 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 | 22 | |
| <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 | 972 – 974 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 977 – 979 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 980 – 1006 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1007 – 1009 | 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 | 1010 – 1012 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1013 – 1045 | 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 | 33 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q05397 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q05397 |
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 | Q05397 |
<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 | 35 – 355 | FERMPROSITE-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 | 321 | |
| <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 | 422 – 680 | Protein kinasePROSITE-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 | 259 |
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 | 707 – 1052 | Interaction with TGFB1I1Add BLAST | 346 | |
| <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 | 912 – 1052 | Interaction with ARHGEF28By similarityAdd BLAST | 141 |
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 | 712 – 733 | Pro-richAdd BLAST | 22 | |
| <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 | 863 – 913 | Pro-richAdd BLAST | 51 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4257 Eukaryota ENOG410ZH9Y LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118799 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000069938 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004018 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q05397 |
KEGG Orthology (KO) More...KOi | K05725 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q05397 |
TreeFam database of animal gene trees More...TreeFami | TF316643 |
Family and domain databases
Conserved Domains Database More...CDDi | cd14473 FERM_B-lobe, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.80.10, 1 hit 2.30.29.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR019749 Band_41_domain IPR014352 FERM/acyl-CoA-bd_prot_sf IPR035963 FERM_2 IPR019748 FERM_central IPR000299 FERM_domain IPR036137 Focal_adhe_kin_target_dom_sf IPR005189 Focal_adhesion_kin_target_dom IPR011009 Kinase-like_dom_sf IPR011993 PH-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom IPR029071 Ubiquitin-like_domsf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00373 FERM_M, 1 hit PF03623 Focal_AT, 1 hit PF07714 Pkinase_Tyr, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00109 TYRKINASE |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD006413 Focal_adhesion_target_reg, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00295 B41, 1 hit SM00219 TyrKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47031 SSF47031, 1 hit SSF54236 SSF54236, 1 hit SSF56112 SSF56112, 1 hit SSF68993 SSF68993, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00661 FERM_2, 1 hit PS50057 FERM_3, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00109 PROTEIN_KINASE_TYR, 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 (7)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.
<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 7 <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 promoter usage and alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT
60 70 80 90 100
TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV
110 120 130 140 150
DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190 200
VKSDYMLEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA
460 470 480 490 500
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME
510 520 530 540 550
LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590 600
NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
610 620 630 640 650
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT
660 670 680 690 700
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS
760 770 780 790 800
HGITAMAGSI YPGQASLLDQ TDSWNHRPQE IAMWQPNVED STVLDLRGIG
810 820 830 840 850
QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS
860 870 880 890 900
LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE
910 920 930 940 950
GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY
960 970 980 990 1000
VPMVKEVGLA LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK
1010 1020 1030 1040 1050
MKLAQQYVMT SLQQEYKKQM LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR
PH
The sequence of this isoform differs from the canonical sequence as follows:
1-181: Missing.
182-189: EMRGNALE → MSDYWVVG
472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
834-854: Missing.
10 20 30 40 50
MSDYWVVGKK SNYEVLEKDV GLKRFFPKSL LDSVKAKTLR KLIQQTFRQF
60 70 80 90 100
ANLNREESIL KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS
110 120 130 140 150
YLTDKGCNPT HLADFTQVQT IQYSNSEDKD RKGMLQLKIA GAPEPLTVTA
160 170 180 190 200
PSLTIAENMA DLIDGYCRLV NGTSQSFIIR PQKEGERALP SIPKLANSEK
210 220 230 240 250
QGMRTHAVSV SETDDYAEII DEEDTYTMPS TRDYEIQRER IELGRCIGEG
260 270 280 290 300
QFGDVHQGIY MSPENPALAV AIKTCKNCTS DSVREKFLQE ACHYTSLHWN
310 320 330 340 350
WCRYISDPNV DACPDPRNAE LTMRQFDHPH IVKLIGVITE NPVWIIMELC
360 370 380 390 400
TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV
410 420 430 440 450
LVSSNDCVKL GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA
460 470 480 490 500
SDVWMFGVCM WEILMHGVKP FQGVKNNDVI GRIENGERLP MPPNCPPTLY
510 520 530 540 550
SLMTKCWAYD PSRRPRFTEL KAQLSTILEE EKAQQEERMR MESRRQATVS
560 570 580 590 600
WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY QVSGYPGSHG
610 620 630 640 650
ITAMAGSIYP GQASLLDQTD SWNHRPQEIA MWQPNVEDST VLDLRGIGQV
660 670 680 690 700
LPTHLMEERL IRQQQEMEED QRWLEKEERF LIGNQHIYQP VGKPDPAAPP
710 720 730 740 750
KKPPRPGAPG HLGSLASLSS PADSYNEGVK LQPQEISPPP TANLDRSNDK
760 770 780 790 800
VYENVTGLVK AVIEMSSKIQ PAPPEEYVPM VKEVGLALRT LLATVDETIP
810 820 830 840 850
LLPASTHREI EMAQKLLNSD LGELINKMKL AQQYVMTSLQ QEYKKQMLTA
860 870
AHALAVDAKN LLDVIDQARL KMLGQTRPH
The sequence of this isoform differs from the canonical sequence as follows:
1-181: Missing.
182-189: EMRGNALE → MSDYWVVG
472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
677-706: STILEEEKAQQEERMRMESRRQATVSWDSG → FQNPAQMLPASGRLPNQPCPERENYSFATF
707-1052: Missing.
10 20 30 40 50
MSDYWVVGKK SNYEVLEKDV GLKRFFPKSL LDSVKAKTLR KLIQQTFRQF
60 70 80 90 100
ANLNREESIL KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS
110 120 130 140 150
YLTDKGCNPT HLADFTQVQT IQYSNSEDKD RKGMLQLKIA GAPEPLTVTA
160 170 180 190 200
PSLTIAENMA DLIDGYCRLV NGTSQSFIIR PQKEGERALP SIPKLANSEK
210 220 230 240 250
QGMRTHAVSV SETDDYAEII DEEDTYTMPS TRDYEIQRER IELGRCIGEG
260 270 280 290 300
QFGDVHQGIY MSPENPALAV AIKTCKNCTS DSVREKFLQE ACHYTSLHWN
310 320 330 340 350
WCRYISDPNV DACPDPRNAE LTMRQFDHPH IVKLIGVITE NPVWIIMELC
360 370 380 390 400
TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV
410 420 430 440 450
LVSSNDCVKL GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA
460 470 480 490 500
SDVWMFGVCM WEILMHGVKP FQGVKNNDVI GRIENGERLP MPPNCPPTLY
510 520 530 540 550
SLMTKCWAYD PSRRPRFTEL KAQLFQNPAQ MLPASGRLPN QPCPERENYS
FATF
The sequence of this isoform differs from the canonical sequence as follows:
1-181: Missing.
182-189: EMRGNALE → MSDYWVVG
472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
579-583: ASKGK → GKKSG
584-1052: Missing.
10 20 30 40 50
MSDYWVVGKK SNYEVLEKDV GLKRFFPKSL LDSVKAKTLR KLIQQTFRQF
60 70 80 90 100
ANLNREESIL KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS
110 120 130 140 150
YLTDKGCNPT HLADFTQVQT IQYSNSEDKD RKGMLQLKIA GAPEPLTVTA
160 170 180 190 200
PSLTIAENMA DLIDGYCRLV NGTSQSFIIR PQKEGERALP SIPKLANSEK
210 220 230 240 250
QGMRTHAVSV SETDDYAEII DEEDTYTMPS TRDYEIQRER IELGRCIGEG
260 270 280 290 300
QFGDVHQGIY MSPENPALAV AIKTCKNCTS DSVREKFLQE ACHYTSLHWN
310 320 330 340 350
WCRYISDPNV DACPDPRNAE LTMRQFDHPH IVKLIGVITE NPVWIIMELC
360 370 380 390 400
TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV
410 420 430
LVSSNDCVKL GDFGLSRYME DSTYYKGKKS G
The sequence of this isoform differs from the canonical sequence as follows:
868-868: D → GKEEKNWAERN
903-903: K → KPWR
10 20 30 40 50
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT
60 70 80 90 100
TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV
110 120 130 140 150
DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190 200
VKSDYMLEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA
460 470 480 490 500
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME
510 520 530 540 550
LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590 600
NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
610 620 630 640 650
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT
660 670 680 690 700
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS
760 770 780 790 800
HGITAMAGSI YPGQASLLDQ TDSWNHRPQE IAMWQPNVED STVLDLRGIG
810 820 830 840 850
QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS
860 870 880 890 900
LQGPIGNQHI YQPVGKPGKE EKNWAERNPA APPKKPPRPG APGHLGSLAS
910 920 930 940 950
LSSPADSYNE GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE
960 970 980 990 1000
MSSKIQPAPP EEYVPMVKEV GLALRTLLAT VDETIPLLPA STHREIEMAQ
1010 1020 1030 1040 1050
KLLNSDLGEL INKMKLAQQY VMTSLQQEYK KQMLTAAHAL AVDAKNLLDV
1060
IDQARLKMLG QTRPH
The sequence of this isoform differs from the canonical sequence as follows:
1-692: Missing.
10 20 30 40 50
MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY
60 70 80 90 100
QVSGYPGSHG ITAMAGSIYP GQASLLDQTD SWNHRPQEIA MWQPNVEDST
110 120 130 140 150
VLDLRGIGQV LPTHLMEERL IRQQQEMEED QRWLEKEERF LKPDVRLSRG
160 170 180 190 200
SIDREDGSLQ GPIGNQHIYQ PVGKPDPAAP PKKPPRPGAP GHLGSLASLS
210 220 230 240 250
SPADSYNEGV KLQPQEISPP PTANLDRSND KVYENVTGLV KAVIEMSSKI
260 270 280 290 300
QPAPPEEYVP MVKEVGLALR TLLATVDETI PLLPASTHRE IEMAQKLLNS
310 320 330 340 350
DLGELINKMK LAQQYVMTSL QQEYKKQMLT AAHALAVDAK NLLDVIDQAR
360
LKMLGQTRPH
The sequence of this isoform differs from the canonical sequence as follows:
744-789: Missing.
10 20 30 40 50
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT
60 70 80 90 100
TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV
110 120 130 140 150
DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190 200
VKSDYMLEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA
460 470 480 490 500
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME
510 520 530 540 550
LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590 600
NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
610 620 630 640 650
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT
660 670 680 690 700
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQDSTVLDL
760 770 780 790 800
RGIGQVLPTH LMEERLIRQQ QEMEEDQRWL EKEERFLKPD VRLSRGSIDR
810 820 830 840 850
EDGSLQGPIG NQHIYQPVGK PDPAAPPKKP PRPGAPGHLG SLASLSSPAD
860 870 880 890 900
SYNEGVKLQP QEISPPPTAN LDRSNDKVYE NVTGLVKAVI EMSSKIQPAP
910 920 930 940 950
PEEYVPMVKE VGLALRTLLA TVDETIPLLP ASTHREIEMA QKLLNSDLGE
960 970 980 990 1000
LINKMKLAQQ YVMTSLQQEY KKQMLTAAHA LAVDAKNLLD VIDQARLKML
GQTRPH
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 | 184 | R → L in BAG65198 (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 | 211 | L → I in BAG65198 (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 | 778 | P → S in AAA35819 (PubMed:8422239).Curated | 1 |
Natural variant
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042168 | 1 – 692 | Missing in isoform 6. CuratedAdd BLAST | 692 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004967 | 1 – 181 | Missing in isoform 2, isoform 3 and isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 181 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004968 | 182 – 189 | EMRGNALE → MSDYWVVG in isoform 2, isoform 3 and isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 8 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004969 | 472 | A → ACHYTSLHWNWCRYISDPNV DACPDPRNAE in isoform 2, isoform 3 and isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004971 | 579 – 583 | ASKGK → GKKSG in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 5 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004972 | 584 – 1052 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 469 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004973 | 677 – 706 | STILE…SWDSG → FQNPAQMLPASGRLPNQPCP ERENYSFATF in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 30 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004974 | 707 – 1052 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 346 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057268 | 744 – 789 | Missing in isoform 7. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 46 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004970 | 834 – 854 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 21 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042169 | 868 | D → GKEEKNWAERN in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042170 | 903 | K → KPWR in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L13616 mRNA Translation: AAA58469.1 L05186 mRNA Translation: AAA35819.1 AK304356 mRNA Translation: BAG65198.1 AC067931 Genomic DNA No translation available. AC100860 Genomic DNA No translation available. AC105009 Genomic DNA No translation available. AC105235 Genomic DNA No translation available. KF458878 Genomic DNA No translation available. KF458882 Genomic DNA No translation available. BC035404 mRNA Translation: AAH35404.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS56557.1 [Q05397-5] CCDS6381.1 [Q05397-1] |
Protein sequence database of the Protein Information Resource More...PIRi | I53012 PC1225 |
NCBI Reference Sequences More...RefSeqi | NP_001186578.1, NM_001199649.1 [Q05397-5] NP_722560.1, NM_153831.3 [Q05397-1] XP_016869162.1, XM_017013673.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.395482 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000340930; ENSP00000341189; ENSG00000169398 [Q05397-5] ENST00000395218; ENSP00000378644; ENSG00000169398 [Q05397-7] ENST00000521059; ENSP00000429474; ENSG00000169398 [Q05397-1] ENST00000522684; ENSP00000429911; ENSG00000169398 [Q05397-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5747 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5747 |
UCSC genome browser More...UCSCi | uc003yvu.4 human [Q05397-1] |
<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 promoter usage, 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 | |
|---|---|---|---|---|---|
| Q05397-6 | PTK2 isoform 13 | 362 | |||
| cDNA FLJ57218, highly similar to Focal adhesion kinase 1 (EC 2.7.10.2) | 362 | ||||
| UPI0008F48CB5 | 1137 | ||||
| UPI000D5010A7 | 1093 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q05397 | UPI0005D0203E | 1103 | |||
| UPI0008DB7A3C | 1199 | ||||
| UPI0005D09AA6 | 1126 | ||||
| UPI0005FAA6EF | 1125 | ||||
| UPI0003501BF4 | 1125 | ||||
| +723 | |||||
| Q05397-6 | Focal adhesion kinase 1 | ) | 1090 | ||
| UPI0008DB6F87 | 1226 | ||||
| UPI0005FB1A29 | 1153 | ||||
| UPI0005D0BEC3 | 1147 | ||||
| UPI000905358E | 1143 | ||||
| +375 | |||||
| Q05397-7 | Focal adhesion kinase 1 (Fragment) | 1017 | |||
| UPI0006B11C10 | 1062 | ||||
| UPI00034FAA13 | 1050 | ||||
| UPI00044037B8 | 1050 | ||||
| UPI0006976746 | 1050 | ||||
| +41 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q05397 | UPI0005D0203E | 1103 | |||
| UPI0008DB7A3C | 1199 | ||||
| UPI0005D09AA6 | 1126 | ||||
| UPI0005FAA6EF | 1125 | ||||
| UPI0003501BF4 | 1125 | ||||
| +1765 | |||||
| Q05397-2 | UPI000B7B01A3 | 851 | |||
| UPI0006B1828E | 654 | ||||
| Protein tyrosine kinase 2, transcript variant X1 | 757 | ||||
| UPI00042BA740 | 748 | ||||
| UPI000511531A | 739 | ||||
| +12 | |||||
| Q05397-7 | Focal adhesion kinase 1 (Fragment) | 1017 | |||
| UPI0006B11C10 | 1062 | ||||
| UPI0006976746 | 1050 | ||||
| UPI00034FAA13 | 1050 | ||||
| UPI000A1BD298 | 1050 | ||||
| +259 | |||||
<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
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L13616 mRNA Translation: AAA58469.1 L05186 mRNA Translation: AAA35819.1 AK304356 mRNA Translation: BAG65198.1 AC067931 Genomic DNA No translation available. AC100860 Genomic DNA No translation available. AC105009 Genomic DNA No translation available. AC105235 Genomic DNA No translation available. KF458878 Genomic DNA No translation available. KF458882 Genomic DNA No translation available. BC035404 mRNA Translation: AAH35404.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS56557.1 [Q05397-5] CCDS6381.1 [Q05397-1] |
Protein sequence database of the Protein Information Resource More...PIRi | I53012 PC1225 |
NCBI Reference Sequences More...RefSeqi | NP_001186578.1, NM_001199649.1 [Q05397-5] NP_722560.1, NM_153831.3 [Q05397-1] XP_016869162.1, XM_017013673.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.395482 |
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 |
| 1K04 | X-ray | 1.95 | A | 891-1052 | [»] | |
| 1K05 | X-ray | 2.90 | A/B/C | 891-1052 | [»] | |
| 1MP8 | X-ray | 1.60 | A | 411-686 | [»] | |
| 1OW6 | X-ray | 2.35 | A/B/C | 892-1052 | [»] | |
| 1OW7 | X-ray | 2.60 | A/B/C | 892-1052 | [»] | |
| 1OW8 | X-ray | 2.85 | A/B/C | 892-1052 | [»] | |
| 2ETM | X-ray | 2.30 | A/B | 411-689 | [»] | |
| 2IJM | X-ray | 2.19 | A/B | 411-689 | [»] | |
| 3B71 | X-ray | 2.82 | A/B/C | 891-1052 | [»] | |
| 3BZ3 | X-ray | 2.20 | A | 414-689 | [»] | |
| 3PXK | X-ray | 1.79 | A/B | 411-689 | [»] | |
| 3S9O | X-ray | 2.60 | A/B/C | 891-1052 | [»] | |
| 4EBV | X-ray | 1.67 | A | 411-686 | [»] | |
| 4EBW | X-ray | 2.65 | A | 411-686 | [»] | |
| 4GU6 | X-ray | 1.95 | A/B | 411-689 | [»] | |
| 4GU9 | X-ray | 2.40 | A/B | 410-686 | [»] | |
| 4I4E | X-ray | 1.55 | A | 411-686 | [»] | |
| 4I4F | X-ray | 1.75 | A | 411-686 | [»] | |
| 4K8A | X-ray | 2.91 | A/B | 410-686 | [»] | |
| 4K9Y | X-ray | 2.00 | A | 410-686 | [»] | |
| 4KAB | X-ray | 2.71 | A/B | 410-686 | [»] | |
| 4KAO | X-ray | 2.39 | A/B | 410-689 | [»] | |
| 4NY0 | X-ray | 2.80 | A/B/C/D | 31-405 | [»] | |
| 4Q9S | X-ray | 2.07 | A | 411-686 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q05397 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q05397 | |||||
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 | 111719, 126 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q05397 |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q05397 |
Protein interaction database and analysis system More...IntActi | Q05397, 70 interactors |
Molecular INTeraction database More...MINTi | Q05397 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000341189 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q05397 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2695 |
Drug and drug target database More...DrugBanki | DB07460 2-({5-CHLORO-2-[(2-METHOXY-4-MORPHOLIN-4-YLPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)-N-METHYLBENZAMIDE |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2180 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | Q05397 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q05397 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q05397 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PTK2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 3183518 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q05397 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q05397 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q05397 |
PeptideAtlas More...PeptideAtlasi | Q05397 |
PRoteomics IDEntifications database More...PRIDEi | Q05397 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 58320 58321 [Q05397-2] 58322 [Q05397-3] 58323 [Q05397-4] 58324 [Q05397-5] 58325 [Q05397-6] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5747 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000340930; ENSP00000341189; ENSG00000169398 [Q05397-5] ENST00000395218; ENSP00000378644; ENSG00000169398 [Q05397-7] ENST00000521059; ENSP00000429474; ENSG00000169398 [Q05397-1] ENST00000522684; ENSP00000429911; ENSG00000169398 [Q05397-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5747 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5747 |
UCSC genome browser More...UCSCi | uc003yvu.4 human [Q05397-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5747 |
DisGeNET More...DisGeNETi | 5747 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000169398.19 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PTK2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9611 PTK2 |
Human Protein Atlas More...HPAi | CAB004036 HPA001842 HPA029671 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600758 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q05397 |
Open Targets More...OpenTargetsi | ENSG00000169398 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33955 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4257 Eukaryota ENOG410ZH9Y LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118799 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000069938 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004018 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q05397 |
KEGG Orthology (KO) More...KOi | K05725 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q05397 |
TreeFam database of animal gene trees More...TreeFami | TF316643 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.2 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-111465 Apoptotic cleavage of cellular proteins R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-354192 Integrin alphaIIb beta3 signaling R-HSA-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins R-HSA-372708 p130Cas linkage to MAPK signaling for integrins R-HSA-375165 NCAM signaling for neurite out-growth R-HSA-391160 Signal regulatory protein family interactions R-HSA-3928662 EPHB-mediated forward signaling R-HSA-418885 DCC mediated attractive signaling R-HSA-418886 Netrin mediated repulsion signals R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs R-HSA-5673001 RAF/MAP kinase cascade R-HSA-8874081 MET activates PTK2 signaling |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q05397 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q05397 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PTK2 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q05397 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | PTK2 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5747 |
CutDB - Proteolytic event database More...PMAP-CutDBi | Q05397 |
Protein Ontology More...PROi | PR:Q05397 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000169398 |
CleanEx database of gene expression profiles More...CleanExi | HS_PTK2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q05397 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q05397 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd14473 FERM_B-lobe, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.80.10, 1 hit 2.30.29.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR019749 Band_41_domain IPR014352 FERM/acyl-CoA-bd_prot_sf IPR035963 FERM_2 IPR019748 FERM_central IPR000299 FERM_domain IPR036137 Focal_adhe_kin_target_dom_sf IPR005189 Focal_adhesion_kin_target_dom IPR011009 Kinase-like_dom_sf IPR011993 PH-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom IPR029071 Ubiquitin-like_domsf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00373 FERM_M, 1 hit PF03623 Focal_AT, 1 hit PF07714 Pkinase_Tyr, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00109 TYRKINASE |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD006413 Focal_adhesion_target_reg, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00295 B41, 1 hit SM00219 TyrKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47031 SSF47031, 1 hit SSF54236 SSF54236, 1 hit SSF56112 SSF56112, 1 hit SSF68993 SSF68993, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00661 FERM_2, 1 hit PS50057 FERM_3, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00109 PROTEIN_KINASE_TYR, 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 | FAK1_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 | Q05397Primary (citable) accession number: Q05397 Secondary accession number(s): B4E2N6 , F5H4S4, J3QT16, Q14291, Q8IYN9, Q9UD85 | |
| <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: | February 1, 1994 |
| Last sequence update: | July 15, 1998 | |
| Last modified: | July 18, 2018 | |
| This is version 221 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 8
Human chromosome 8: 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 - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
