PTK2
entrez
5747
canonical
uniprot
Q05397
canonical
ensembl
ENSG00000169398
resolver
ensp
ENSP00000341189
resolver
ensp
ENSP00000403416
resolver
ensp
ENSP00000427904
resolver
ensp
ENSP00000428492
resolver
ensp
ENSP00000429082
resolver
ensp
ENSP00000429129
resolver
ensp
ENSP00000429911
resolver
ensp
ENSP00000430277
resolver
ensp
ENSP00000430603
resolver
ensp
ENSP00000512868
resolver
ensp
ENSP00000564169
resolver
ensp
ENSP00000564170
resolver
ensp
ENSP00000564172
resolver
ensp
ENSP00000564176
resolver
ensp
ENSP00000564177
resolver
ensp
ENSP00000613816
resolver
ensp
ENSP00000613819
resolver
ensp
ENSP00000613821
resolver
ensp
ENSP00000613822
resolver
ensp
ENSP00000652884
resolver
ensp
ENSP00000652887
resolver
ensp
ENSP00000721963
resolver
ensp
ENSP00000721966
resolver
ensp
ENSP00000721967
resolver
ensp
ENSP00000721968
resolver
ensp
ENSP00000721971
resolver
ensp
ENSP00000721972
resolver
ensp
ENSP00000721976
resolver
ensp
ENSP00000721982
resolver
ensp
ENSP00000721988
resolver
ensp
ENSP00000754440
resolver
ensp
ENSP00000754449
resolver
ensp
ENSP00000783826
resolver
ensp
ENSP00000783828
resolver
enst
ENST00000430260
resolver
enst
ENST00000517887
resolver
enst
ENST00000519419
resolver
enst
ENST00000519881
resolver
enst
ENST00000520892
resolver
enst
ENST00000696786
resolver
genesymbol
PTK2
resolver
genesymbol_syn
FAK
resolver
genesymbol_syn
FAK1
resolver
hgnc
HGNC:9611
resolver
uniprot
A0A8Q3WLM4
resolver
uniprot
B4DWJ1
resolver
uniprot
B4E2N6
resolver
uniprot
E5RFW9
resolver
uniprot
E7ESA6
resolver
uniprot
F5H4S4
resolver
uniprot
F8VSV1
resolver
uniprot
J3QT16
resolver
uniprot
Q14291
resolver
uniprot
Q59GM6
resolver
uniprot
Q59GN8
resolver
uniprot
Q8IYN9
resolver
uniprot
Q9UD85
resolver
uniprot_entry
A0A8Q3WLM4_HUMAN
resolver
uniprot_entry
B4DWJ1_HUMAN
resolver
uniprot_entry
E5RFW9_HUMAN
resolver
uniprot_entry
E7ESA6_HUMAN
resolver
uniprot_entry
F8VSV1_HUMAN
resolver
uniprot_entry
FAK1_HUMAN
resolver
uniprot_entry
Q59GM6_HUMAN
resolver
uniprot_entry
Q59GN8_HUMAN
resolver
uniprot_sec
B4E2N6
resolver
uniprot_sec
F5H4S4
resolver
uniprot_sec
J3QT16
resolver
uniprot_sec
Q14291
resolver
uniprot_sec
Q8IYN9
resolver
uniprot_sec
Q9UD85
resolver
activity_regulation
ACTIVITY REGULATION: Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-562,271. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:20495381}.
uniprot
proteins
amino_acid_sequence
MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
uniprot
proteins
disease_involvement
DISEASE: Note=Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G protein-coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:15166238, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:15895076, ECO:0000269|PubMed:16919435, ECO:0000269|PubMed:16927379, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:17968709, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:19138410, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19224453, ECO:0000269|PubMed:20332118, ECO:0000269|PubMed:20495381, ECO:0000269|PubMed:21454698, ECO:0000269|PubMed:9360983}.; FUNCTION: [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:20109444}.
uniprot
proteins
mass_dalton
119233
uniprot
proteins
mutagenesis
MUTAGEN 397; /note="Y->F: Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. Reduces phosphorylation of NEDD9."; /evidence="ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:9360983"; MUTAGEN 928; /note="V->G: Loss of interaction with TGFB1I1."; /evidence="ECO:0000269|PubMed:9756887"; MUTAGEN 1034; /note="L->S: Loss of interaction with TGFB1I1."; /evidence="ECO:0000269|PubMed:9756887
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity). {ECO:0000250|UniProtKB:P34152, ECO:0000269|PubMed:12387730, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698}.; PTM: Sumoylated; this enhances autophosphorylation. {ECO:0000250}.
uniprot
proteins
protein_family
FAK subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10354709
uniprot
proteins
pubmed
10655584
uniprot
proteins
pubmed
11331870
uniprot
proteins
pubmed
11980671
uniprot
proteins
pubmed
12005431
uniprot
proteins
pubmed
12221124
uniprot
proteins
pubmed
12387730
uniprot
proteins
pubmed
12467573
uniprot
proteins
pubmed
14527389
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15166238
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561106
uniprot
proteins
pubmed
15725728
uniprot
proteins
pubmed
15855171
uniprot
proteins
pubmed
15895076
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
16452200
uniprot
proteins
pubmed
16919435
uniprot
proteins
pubmed
16927379
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
16998626
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17395594
uniprot
proteins
pubmed
17431114
uniprot
proteins
pubmed
17968709
uniprot
proteins
pubmed
18006843
uniprot
proteins
pubmed
18078954
uniprot
proteins
pubmed
18206965
uniprot
proteins
pubmed
18256281
uniprot
proteins
pubmed
18292575
uniprot
proteins
pubmed
18339875
uniprot
proteins
pubmed
18497331
uniprot
proteins
pubmed
18657504
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18677107
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19118217
uniprot
proteins
pubmed
19138410
uniprot
proteins
pubmed
19147981
uniprot
proteins
pubmed
19224453
uniprot
proteins
pubmed
19339212
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19494199
uniprot
proteins
pubmed
19525103
uniprot
proteins
pubmed
19787193
uniprot
proteins
pubmed
19917054
uniprot
proteins
pubmed
20037584
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20101634
uniprot
proteins
pubmed
20109444
uniprot
proteins
pubmed
20332118
uniprot
proteins
pubmed
20439989
uniprot
proteins
pubmed
20495381
uniprot
proteins
pubmed
20515733
uniprot
proteins
pubmed
20552554
uniprot
proteins
pubmed
20798394
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21454698
uniprot
proteins
pubmed
21482413
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23503467
uniprot
proteins
pubmed
23509069
uniprot
proteins
pubmed
29069646
uniprot
proteins
pubmed
31630787
uniprot
proteins
pubmed
7692878
uniprot
proteins
pubmed
8247543
uniprot
proteins
pubmed
8422239
uniprot
proteins
pubmed
9360983
uniprot
proteins
pubmed
9422762
uniprot
proteins
pubmed
9756887
uniprot
proteins
sequence_length
1052
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:31630787}. Cell membrane {ECO:0000250|UniProtKB:Q00944}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00944}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15855171}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O35346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:18206965}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:31630787}. Cytoplasm {ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:18078954, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000250|UniProtKB:P34152}.
uniprot
proteins