Ptk2
entrez
14083
canonical
uniprot
P34152
canonical
ensembl
ENSMUSG00000022607
resolver
ensp
ENSMUSP00000105663
resolver
ensp
ENSMUSP00000154242
resolver
ensp
ENSMUSP00000159174
resolver
ensp
ENSMUSP00000224516
resolver
genesymbol
Ptk2
resolver
genesymbol_syn
Fadk
resolver
genesymbol_syn
Fak
resolver
genesymbol_syn
Fak1
resolver
genesymbol_syn
Kiaa4203
resolver
uniprot
K7Q751
resolver
uniprot
O08578
resolver
uniprot
Q5DTH7
resolver
uniprot
Q8C513
resolver
uniprot
Q8CFH7
resolver
uniprot
Q8CHM2
resolver
uniprot
Q8K2S0
resolver
uniprot
Q9DAW3
resolver
uniprot_entry
FAK1_MOUSE
resolver
uniprot_entry
K7Q751_MOUSE
resolver
uniprot_sec
O08578
resolver
uniprot_sec
Q5DTH7
resolver
uniprot_sec
Q8C513
resolver
uniprot_sec
Q8CFH7
resolver
uniprot_sec
Q8CHM2
resolver
uniprot_sec
Q8K2S0
resolver
uniprot_sec
Q9DAW3
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 by SRC. Phosphorylation at Tyr-397, Tyr-576 and Tyr-577 is required for maximal kinase activity. {ECO:0000269|PubMed:7529876}.
uniprot
proteins
amino_acid_sequence
MAAAYLDPNLNHTPSSSTKTHLGTGMERSPGAMERVLKVFHYFESSSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMQEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGIPAMAGSIYQGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPALPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
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:25059660). 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. {ECO:0000250|UniProtKB:Q05397, ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:10806474, ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11369769, ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:15967814, ECO:0000269|PubMed:16000375, ECO:0000269|PubMed:16391003, ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:22056317, ECO:0000269|PubMed:25059660, ECO:0000269|PubMed:7478517, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:9148935}.; FUNCTION: [Isoform 9]: 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 (By similarity). {ECO:0000250|UniProtKB:Q05397}.
uniprot
proteins
mass_dalton
119243
uniprot
proteins
mutagenesis
MUTAGEN 397; /note="Y->F: Strongly reduced enzyme activity; when associated with 576-F-F-577. Abolishes activation of MAPK1/ERK2 in response to integrin signaling. Abolishes activation of SRC. Abolishes interaction with PIK3R1."; /evidence="ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:7529876, ECO:0000269|PubMed:8824286"; MUTAGEN 576..577; /note="YY->FF: Strongly reduced enzyme activity; when associated with F-397."; /evidence="ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:7529876"; MUTAGEN 925; /note="Y->F: Abolishes interaction with GRB2."; /evidence="ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8816475"; MUTAGEN 1034; /note="L->S: Loss of interaction with ARHGEF28."; /evidence="ECO:0000269|PubMed:12702722
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 (PubMed:22685302). {ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:10806474, ECO:0000269|PubMed:11420674, ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:14676198, ECO:0000269|PubMed:1528852, ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:7529876, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8816475, ECO:0000269|PubMed:8824286, ECO:0000269|PubMed:9148935, ECO:0000269|Ref.6}.; 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
10373530
uniprot
proteins
pubmed
10806474
uniprot
proteins
pubmed
10896938
uniprot
proteins
pubmed
11278462
uniprot
proteins
pubmed
11369769
uniprot
proteins
pubmed
11420674
uniprot
proteins
pubmed
11799401
uniprot
proteins
pubmed
12221124
uniprot
proteins
pubmed
12464388
uniprot
proteins
pubmed
12674328
uniprot
proteins
pubmed
12702722
uniprot
proteins
pubmed
12941275
uniprot
proteins
pubmed
14500712
uniprot
proteins
pubmed
14676198
uniprot
proteins
pubmed
1528852
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15494733
uniprot
proteins
pubmed
15494734
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15967814
uniprot
proteins
pubmed
16000375
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16391003
uniprot
proteins
pubmed
17093062
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
18206965
uniprot
proteins
pubmed
19147981
uniprot
proteins
pubmed
19372463
uniprot
proteins
pubmed
19473962
uniprot
proteins
pubmed
20552554
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21482413
uniprot
proteins
pubmed
22056317
uniprot
proteins
pubmed
22685302
uniprot
proteins
pubmed
25059660
uniprot
proteins
pubmed
28362576
uniprot
proteins
pubmed
7478517
uniprot
proteins
pubmed
7529876
uniprot
proteins
pubmed
7622520
uniprot
proteins
pubmed
7997267
uniprot
proteins
pubmed
8816475
uniprot
proteins
pubmed
8824286
uniprot
proteins
pubmed
9148935
uniprot
proteins
pubmed
9353341
uniprot
proteins
pubmed
9422762
uniprot
proteins
pubmed
9461600
uniprot
proteins
pubmed
9756887
uniprot
proteins
sequence_length
1052
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:1528852}. 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:12941275}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O35346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus {ECO:0000269|PubMed:18206965}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q05397}. Cytoplasm {ECO:0000269|PubMed:18206965}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000269|PubMed:12941275}.
uniprot
proteins