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Collapse Statistics
226 human active and 11 inactive phosphatases in total;
194 phosphatases have substrate data;
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305 protein substrates;
89 non-protein substrates;
1114 dephosphorylation interactions;
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213 KEGG pathways;
206 NCI Nature PID pathways
560 Reactome pathways;
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last update: 18 Feb, 2016

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FAK

Gene Name PTK2 (QuickGO)

PDB ID: 1K04
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SynonymsPTK2 FAK FAK1
Protein NameFAK
Alternative Name(s)
Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Protein-tyrosine kinase 2) (pp125FAK)
Protein FamilyProtein kinase superfamily, Tyr protein kinase family, FAK subfamily
EntrezGene ID5747
UniProt AC (Human)Q05397 (protein sequence)
Enzyme ClassEC 2.7.10.2 (BRENDA )
Molecular Weight119233
Protein Length1052
Protein DomainInterPro | Pfam3D Structure * PDB | PDBe | DrugPort
* ModBase | SwissModel
Localization (UniProt annotation)Cell junction > focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Gene ExpressionGene Expression Atlas Function and DiseaseOMIM
Protein-protein Interaction Database STRING | IntAct | MINT
Kinase Database Phospho.ELM | PhosphoSite | NetworKIN
Function (UniProt annotation)
FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly. Plays a potential role in oncogenic transformations resulting in increased kinase activity.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Protein Sequence
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGITAMAGSI YPGQASLLDQ TDSWNHRPQE IAMWQPNVED STVLDLRGIG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK MKLAQQYVMT SLQQEYKKQM LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH
ELM motif
DOC_WW_Pin1_4The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase.
LIG_SH2_SRCSrc-family Src Homology 2 (SH2) domains binding motif.
LIG_SH3_2This is the motif recognized by class II SH3 domains
MOD_ProDKin_1Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes.
Gene Ontology
GO:0005524ATP binding
GO:0008432JUN kinase binding
GO:0042169SH2 domain binding
GO:0007411axon guidance
GO:0007596blood coagulation
GO:0006921cellular component disassembly involved in apoptosis
GO:0005856cytoskeleton
GO:0005829cytosol
GO:0048013ephrin receptor signaling pathway
GO:0005925focal adhesion
GO:0060396growth hormone receptor signaling pathway
GO:0007229integrin-mediated signaling pathway
GO:0004715non-membrane spanning protein tyrosine kinase activity
GO:0018108peptidyl-tyrosine phosphorylation
GO:0046777protein autophosphorylation
GO:0033628regulation of cell adhesion mediated by integrin
GO:0007172signal complex assembly
GO:0004871signal transducer activity

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