Ptk2b
entrez
19229
canonical
uniprot
Q9QVP9
canonical
ensembl
ENSMUSG00000059456
resolver
ensp
ENSMUSP00000022622
resolver
ensp
ENSMUSP00000086661
resolver
ensp
ENSMUSP00000106750
resolver
ensp
ENSMUSP00000137008
resolver
ensp
ENSMUSP00000173731
resolver
ensp
ENSMUSP00000173759
resolver
enst
ENSMUST00000022622
resolver
enst
ENSMUST00000089250
resolver
enst
ENSMUST00000111121
resolver
enst
ENSMUST00000178730
resolver
genesymbol
Ptk2b
resolver
genesymbol_syn
Fak2
resolver
genesymbol_syn
Pyk2
resolver
genesymbol_syn
Raftk
resolver
uniprot
B2RQ16
resolver
uniprot
E9Q2A6
resolver
uniprot
F6X9G5
resolver
uniprot
G3X8V1
resolver
uniprot
K7QD41
resolver
uniprot
Q3UDE9
resolver
uniprot_entry
E9Q2A6_MOUSE
resolver
uniprot_entry
F6X9G5_MOUSE
resolver
uniprot_entry
FAK2_MOUSE
resolver
uniprot_entry
K7QD41_MOUSE
resolver
uniprot_entry
Q3UDE9_MOUSE
resolver
uniprot_sec
B2RQ16
resolver
uniprot_sec
G3X8V1
resolver
activity_regulation
ACTIVITY REGULATION: Activated in response to stimuli that lead to increased intracellular Ca(2+) levels; this activation is indirect and may be mediated by calcium-mediated production of reactive oxygen species (ROS). Activated by autophosphorylation at Tyr-402; this creates a binding site for SRC family kinases and leads to phosphorylation at additional tyrosine residues. Phosphorylation at Tyr-402, Tyr-579 and Tyr-580 is required for optimal kinase activity. {ECO:0000269|PubMed:17537919, ECO:0000269|PubMed:20688918}.
uniprot
proteins
amino_acid_sequence
MSGVSEPLSRVKVGTLRRPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIKSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIMHAKKDGEKRNSLPQIPTLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGVAREEVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTQDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVPTLVLYTLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMEKDIAIEQERNARYRPPKILEPTTFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAEKIKMKQVLERQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYHNVMTLVEAVLELKNKLGQLPPEDYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMKLAQQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G protein-coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. 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 of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9', 'Tyr-373', and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10881171, ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:12960403, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:17537919, ECO:0000269|PubMed:17698736, ECO:0000269|PubMed:17846174, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:19561089, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20688918, ECO:0000269|PubMed:21640103}.
uniprot
proteins
mass_dalton
115794
uniprot
proteins
mutagenesis
MUTAGEN 402; /note="Y->A: Loss of phosphorylation and interaction with SRC, and inhibition of bone resorption."; /evidence="ECO:0000269|PubMed:14739300
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration; this activation is indirect and may be mediated by production of reactive oxygen species (ROS). Tyr-402 is the major autophosphorylation site, but other kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-402 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is important for interaction with GRB2. Phosphorylated on tyrosine residues upon activation of FGR and PKC. Recruitment by NPHP1 to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity. Phosphorylation by MYLK promotes ITGB2 activation and is thus essential to trigger neutrophil transmigration during lung injury. Dephosphorylated by PTPN12 (By similarity). {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
10469599
uniprot
proteins
pubmed
10881171
uniprot
proteins
pubmed
11238453
uniprot
proteins
pubmed
11420674
uniprot
proteins
pubmed
11493697
uniprot
proteins
pubmed
12486027
uniprot
proteins
pubmed
12674328
uniprot
proteins
pubmed
12960403
uniprot
proteins
pubmed
14739300
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561106
uniprot
proteins
pubmed
17537919
uniprot
proteins
pubmed
17698736
uniprot
proteins
pubmed
17846174
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
18587400
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19561089
uniprot
proteins
pubmed
19880522
uniprot
proteins
pubmed
20688918
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21195757
uniprot
proteins
pubmed
21640103
uniprot
proteins
pubmed
7499242
uniprot
proteins
pubmed
8940124
uniprot
proteins
pubmed
9422762
uniprot
proteins
sequence_length
1009
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery (By similarity). Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts. {ECO:0000250}.
uniprot
proteins