HUMAN:FAK1

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Species (Taxon ID)	Homo sapiens (Human). ([1])
Gene Name(s)	PTK2 (synonyms: FAK, FAK1)
Protein Name(s)	Focal adhesion kinase 1 FADK 1 Protein-tyrosine kinase 2 pp125FAK
External Links
EMBL	L13616 L05186 AC067931 AC100860 AC105009 AC105235
IPI	IPI00216217 IPI00216218 IPI00982478 IPI01011193
PIR	I53012 PC1225
RefSeq	NP_722560.1
UniGene	Hs.395482
PDB	1K04 1K05 1MP8 1OW6 1OW7 1OW8 2ETM 2IJM 2RA7 3B71 3BZ3
PDBsum	1K04 1K05 1MP8 1OW6 1OW7 1OW8 2ETM 2IJM 2RA7 3B71 3BZ3
ProteinModelPortal	Q05397
SMR	Q05397
IntAct	Q05397
MINT	MINT-92695
STRING	Q05397
PhosphoSite	Q05397
PRIDE	Q05397
Ensembl	ENST00000340930 ENST00000395223
GeneID	5747
KEGG	hsa:5747
UCSC	uc003yvt.1
CTD	5747
GeneCards	GC08M136979
H-InvDB	HIX0020601
HGNC	HGNC:9611
HPA	CAB004036 HPA001842
MIM	600758
neXtProt	NX_Q05397
PharmGKB	PA33955
eggNOG	prNOG18315
GeneTree	ENSGT00600000084269
HOVERGEN	HBG004018
InParanoid	Q05397
OrthoDB	EOG4WH8K1
PhylomeDB	Q05397
BRENDA	2.7.10.2
Pathway_Interaction_DB	angiopoietinreceptor_pathway caspase_pathway epha2_fwdpathway ephbfwdpathway fcer1pathway igf1_pathway avb3_integrin_pathway lysophospholipid_pathway a4b1_paxindep_pathway met_pathway vegfr1_2_pathway ret_pathway syndecan_4_pathway
Reactome	REACT_13552 REACT_18266 REACT_20676 REACT_23853 REACT_578 REACT_604
NextBio	22380
PMAP-CutDB	Q05397
ArrayExpress	Q05397
Bgee	Q05397
CleanEx	HS_PTK2
Genevestigator	Q05397
GermOnline	ENSG00000169398
GO	GO:0005856 GO:0005829 GO:0005925 GO:0005524 GO:0008432 GO:0004715 GO:0042169 GO:0004871 GO:0007411 GO:0007596 GO:0006921 GO:0048013 GO:0060396 GO:0007229 GO:0018108 GO:0046777 GO:0033628 GO:0007172
InterPro	IPR019749 IPR014352 IPR019748 IPR000299 IPR005189 IPR011009 IPR000719 IPR017441 IPR001245 IPR008266 IPR020635
Gene3D	G3DSA:1.20.80.10
Pfam	PF00373 PF03623 PF07714
PRINTS	PR00109
ProDom	PD006413
SMART	SM00295 SM00219
SUPFAM	SSF47031 SSF68993 SSF56112
PROSITE	PS00660 PS00661 PS50057 PS00107 PS50011 PS00109

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	F	Seeded From UniProt
	GO:0004672	protein kinase activity	Reactome:REACT_15535	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005189	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020635	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0829	F	Seeded From UniProt
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.10.2	F	Seeded From UniProt
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	PMID:10655584^[1]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004871	signal transducer activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005189	F	Seeded From UniProt
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR014352	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10655584^[1]	IPI: Inferred from Physical Interaction	UniProtKB:P29317	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10822899^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P35579	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11331870^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P51813	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:14688263^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q15654	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15855171^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P04637	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16291744^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P12931	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19732724^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q68CZ2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21034468^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P49023	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:8649368^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P56945	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9756887^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q62219	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9786953^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P54939	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:18029348^[12]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_12021	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15323	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15348	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15368	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15371	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15375	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15397	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15405	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15535	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_18259	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_18366	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_18375	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22183	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22199	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22200	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22213	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22278	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22281	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22309	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005856	cytoskeleton	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000299	C	Seeded From UniProt
	GO:0005856	cytoskeleton	PMID:10801330^[13]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C	Seeded From UniProt
	GO:0005925	focal adhesion	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005189	C	Seeded From UniProt
	GO:0005925	focal adhesion	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0118	C	Seeded From UniProt
	GO:0005925	focal adhesion	PMID:10655584^[1]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005925	focal adhesion	PMID:18029348^[12]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005189	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	Reactome:REACT_15535	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006915	apoptosis	Reactome:REACT_578	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006921	cellular component disassembly involved in apoptosis	Reactome:REACT_995	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007165	signal transduction	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005189	P	Seeded From UniProt
	GO:0007172	signal complex assembly	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR005189	P	Seeded From UniProt
	GO:0007229	integrin-mediated signaling pathway	PMID:9636140^[14]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007411	axon guidance	Reactome:REACT_18266	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007596	blood coagulation	Reactome:REACT_604	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0008432	JUN kinase binding	PMID:10925297^[15]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F	Seeded From UniProt
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P	Seeded From UniProt
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F	Seeded From UniProt
	GO:0016772	transferase activity, transferring phosphorus-containing groups	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F	Seeded From UniProt
	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:10655584^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0019901	protein kinase binding	PMID:19118217^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P21709	F	Seeded From UniProt
	GO:0030054	cell junction	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0965	C	Seeded From UniProt
	GO:0033628	regulation of cell adhesion mediated by integrin	PMID:10655584^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0042169	SH2 domain binding	PMID:15077193^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P20936	F	Seeded From UniProt
	GO:0046777	protein autophosphorylation	PMID:10655584^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0048013	ephrin receptor signaling pathway	PMID:10655584^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0060396	growth hormone receptor signaling pathway	PMID:10925297^[15]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	PMID:21703394^[18]	IMP: Inferred from Mutant Phenotype		F	Figure 3B shows that mutation in PTK2 gene that scr protein in autistic lymphoblasts were decreased, in addition there was reduced phosphorylation on the activating site of Src.	complete
	GO:0016477	cell migration	PMID:21703394^[18]	IMP: Inferred from Mutant Phenotype		P	Figure 4A shows 26% decrease in lymphoblasts migration in mutant PTK2 (FAK1) compared to control. Figure 6A over expression of PTK2 rescued reduced migration of B-lymphoblast.	complete
	GO:0007155	cell adhesion	PMID:21703394^[18]	IMP: Inferred from Mutant Phenotype		P	Cell adhesion assay was used, in autistic patients with PTK2 (FAK1) showed lymphoblast adhesion to intercellular adhesion molecule 1 increased, figure 4B. Figure 6B over expression of PTK2, stopped the increase of B lymphoblast adhesion to intercellular adhesion molecule 1. Over expression rescued mutant PTK2 B lymphoblast cells.	complete
	GO:0042113	B cell activation	PMID:21703394^[18]	IMP: Inferred from Mutant Phenotype		P	Fig 4B: Formation and secretion of Igs are natural functions of B lymphoblast cells. Ig production was examined by looking at IgG production. Autistic patients with PTK2 (FAK1)mutation showed decrease in IgG production compared to controls therefore this shows impaired B lymphoblast function.	complete
	GO:0051024	positive regulation of immunoglobulin secretion	PMID:21703394^[18]	IMP: Inferred from Mutant Phenotype		P	Autistic patients who showed decrease in PTK2(FAK1)expression showed decrease in IgG production and secretion compared to controls therefore impairing B lymphoblast cells function compared to control.	complete
	GO:0007229	integrin-mediated signaling pathway	PMID:21703394^[18]	IMP: Inferred from Mutant Phenotype		P	Fig. 7: PTK2(FAK1) has a role in generation of integrin-stimulated signals to downstream targets such as Src, MEK signalling cascades and PI3K-Akt. Therefore when inhibitors were used in each of the targets, PTK2 stimulating effect was blocked which reduced total migration of B lymphoblast by 12.1% in autistic patients,figure 7.	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Miao H et al. (2000) Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat Cell Biol 2: 62-9 PubMed GONUTS page
↑ Sajid M et al. (2000) Protein complexes involving alpha v beta 3 integrins, nonmuscle myosin heavy chain-A, and focal adhesion kinase from in thrombospondin-treated smooth muscle cells. J Investig Med 48: 190-7 PubMed GONUTS page
↑ Chen R et al. (2001) Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain. Nat Cell Biol 3: 439-44 PubMed GONUTS page
↑ Xu J et al. (2004) TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor. J Biol Chem 279: 10459-68 PubMed GONUTS page
↑ Golubovskaya VM et al. (2005) Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53. J Biol Chem 280: 25008-21 PubMed GONUTS page
↑ Zhang Z et al. (2006) Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration. J Biol Chem 281: 1746-54 PubMed GONUTS page
↑ Qian X et al. (2009) The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis. Cancer Cell 16: 246-58 PubMed GONUTS page
↑ Xu M et al. (2010) Cyanidin-3-glucoside inhibits ethanol-induced invasion of breast cancer cells overexpressing ErbB2. Mol Cancer 9: 285 PubMed GONUTS page
↑ Vuori K et al. (1996) Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol Cell Biol 16: 2606-13 PubMed GONUTS page
↑ Fujita H et al. (1998) Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase. J Biol Chem 273: 26516-21 PubMed GONUTS page
↑ Borowsky ML & Hynes RO (1998) Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles. J Cell Biol 143: 429-42 PubMed GONUTS page
↑ ^12.0 ^12.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
↑ Ohmori T et al. (2000) Tyrosine dephosphorylation, but not phosphorylation, of p130Cas is dependent on integrin alpha IIb beta 3-mediated aggregation in platelets: implication of p130Cas involvement in pathways unrelated to cytoskeletal reorganization. Biochemistry 39: 5797-807 PubMed GONUTS page
↑ Slack BE (1998) Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix. Proc Natl Acad Sci U S A 95: 7281-6 PubMed GONUTS page
↑ ^15.0 ^15.1 Ryu H et al. (2000) Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin. J Immunol 165: 2116-23 PubMed GONUTS page
↑ Yamazaki T et al. (2009) EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility. J Cell Sci 122: 243-55 PubMed GONUTS page
↑ Hecker TP et al. (2004) Overexpression of FAK promotes Ras activity through the formation of a FAK/p120RasGAP complex in malignant astrocytoma cells. Oncogene 23: 3962-71 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Wei H et al. (2011) Abnormal cell properties and down-regulated FAK-Src complex signaling in B lymphoblasts of autistic subjects. Am J Pathol 179: 66-74 PubMed GONUTS page

[PMID:10655584-0] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Miao H et al. (2000) Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat Cell Biol 2: 62-9 PubMed GONUTS page

[PMID:10822899-1] Sajid M et al. (2000) Protein complexes involving alpha v beta 3 integrins, nonmuscle myosin heavy chain-A, and focal adhesion kinase from in thrombospondin-treated smooth muscle cells. J Investig Med 48: 190-7 PubMed GONUTS page

[PMID:11331870-2] Chen R et al. (2001) Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain. Nat Cell Biol 3: 439-44 PubMed GONUTS page

[PMID:14688263-3] Xu J et al. (2004) TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor. J Biol Chem 279: 10459-68 PubMed GONUTS page

[PMID:15855171-4] Golubovskaya VM et al. (2005) Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53. J Biol Chem 280: 25008-21 PubMed GONUTS page

[PMID:16291744-5] Zhang Z et al. (2006) Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration. J Biol Chem 281: 1746-54 PubMed GONUTS page

[PMID:19732724-6] Qian X et al. (2009) The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis. Cancer Cell 16: 246-58 PubMed GONUTS page

[PMID:21034468-7] Xu M et al. (2010) Cyanidin-3-glucoside inhibits ethanol-induced invasion of breast cancer cells overexpressing ErbB2. Mol Cancer 9: 285 PubMed GONUTS page

[PMID:8649368-8] Vuori K et al. (1996) Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol Cell Biol 16: 2606-13 PubMed GONUTS page

[PMID:9756887-9] Fujita H et al. (1998) Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase. J Biol Chem 273: 26516-21 PubMed GONUTS page

[PMID:9786953-10] Borowsky ML & Hynes RO (1998) Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles. J Cell Biol 143: 429-42 PubMed GONUTS page

[PMID:18029348-11] 12.0 ^12.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page

[PMID:10801330-12] Ohmori T et al. (2000) Tyrosine dephosphorylation, but not phosphorylation, of p130Cas is dependent on integrin alpha IIb beta 3-mediated aggregation in platelets: implication of p130Cas involvement in pathways unrelated to cytoskeletal reorganization. Biochemistry 39: 5797-807 PubMed GONUTS page

[PMID:9636140-13] Slack BE (1998) Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix. Proc Natl Acad Sci U S A 95: 7281-6 PubMed GONUTS page

[PMID:10925297-14] 15.0 ^15.1 Ryu H et al. (2000) Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin. J Immunol 165: 2116-23 PubMed GONUTS page

[PMID:19118217-15] Yamazaki T et al. (2009) EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility. J Cell Sci 122: 243-55 PubMed GONUTS page

[PMID:15077193-16] Hecker TP et al. (2004) Overexpression of FAK promotes Ras activity through the formation of a FAK/p120RasGAP complex in malignant astrocytoma cells. Oncogene 23: 3962-71 PubMed GONUTS page

[PMID:21703394-17] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Wei H et al. (2011) Abnormal cell properties and down-regulated FAK-Src complex signaling in B lymphoblasts of autistic subjects. Am J Pathol 179: 66-74 PubMed GONUTS page

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HUMAN:FAK1

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