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Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2)

 FAK2_RAT                Reviewed;        1009 AA.
P70600; O88489; Q3T1H4; Q63201;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 173.
RecName: Full=Protein-tyrosine kinase 2-beta;
EC=2.7.10.2;
AltName: Full=Calcium-dependent tyrosine kinase;
Short=CADTK;
AltName: Full=Calcium-regulated non-receptor proline-rich tyrosine kinase;
AltName: Full=Cell adhesion kinase beta;
Short=CAK-beta;
Short=CAKB;
AltName: Full=Focal adhesion kinase 2;
Short=FADK 2;
AltName: Full=Proline-rich tyrosine kinase 2;
Name=Ptk2b; Synonyms=Fak2, Pyk2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
310-334; 553-572; 672-687 AND 989-998.
TISSUE=Liver epithelium;
PubMed=8939945; DOI=10.1074/jbc.271.47.29993;
Yu H., Li X., Marchetto G.S., Dy R., Hunter D., Calvo B., Dawson T.L.,
Wilm M., Anderegg R.J., Graves L.M., Earp H.S.;
"Activation of a novel calcium-dependent protein-tyrosine kinase.
Correlation with c-Jun N-terminal kinase but not mitogen-activated
protein kinase activation.";
J. Biol. Chem. 271:29993-29998(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7673154; DOI=10.1074/jbc.270.36.21206;
Sasaki H., Nagura K., Ishino M., Tobioka H., Kotani K., Sasaki T.;
"Cloning and characterization of cell adhesion kinase beta, a novel
protein-tyrosine kinase of the focal adhesion kinase subfamily.";
J. Biol. Chem. 270:21206-21219(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
AND DOMAIN FAT.
TISSUE=Hippocampus;
PubMed=9645946;
Xiong W.-C., Macklem M., Parsons J.T.;
"Expression and characterization of splice variants of PYK2, a focal
adhesion kinase-related protein.";
J. Cell Sci. 111:1981-1991(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND PHOSPHORYLATION.
PubMed=7544443; DOI=10.1038/376737a0;
Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M.,
Plowman G.D., Rudy B., Schlessinger J.;
"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of
ion channel and MAP kinase functions.";
Nature 376:737-745(1995).
[6]
FUNCTION IN G-PROTEIN COUPLED RECEPTOR SIGNALING AND PHOSPHORYLATION
OF SRC, INTERACTION WITH SRC, AND PHOSPHORYLATION.
PubMed=8849729; DOI=10.1038/383547a0;
Dikic I., Tokiwa G., Lev S., Courtneidge S.A., Schlessinger J.;
"A role for Pyk2 and Src in linking G-protein-coupled receptors with
MAP kinase activation.";
Nature 383:547-550(1996).
[7]
INTERACTION WITH TGFB1I1.
PubMed=9422762; DOI=10.1074/jbc.273.2.1003;
Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T.,
Ishino M., Takahashi S., Suzuki R., Sasaki T.;
"Cell adhesion kinase beta forms a complex with a new member, Hic-5,
of proteins localized at focal adhesions.";
J. Biol. Chem. 273:1003-1014(1998).
[8]
FUNCTION IN ANGIOGENESIS; CELL MIGRATION; CELL SPREADING AND
REORGANIZATION OF THE ACTIN CYTOSKELETON, AND TISSUE SPECIFICITY.
PubMed=11739395; DOI=10.1074/jbc.M110673200;
Tang H., Hao Q., Fitzgerald T., Sasaki T., Landon E.J., Inagami T.;
"Pyk2/CAKbeta tyrosine kinase activity-mediated angiogenesis of
pulmonary vascular endothelial cells.";
J. Biol. Chem. 277:5441-5447(2002).
[9]
INTERACTION WITH KCNA2.
PubMed=11739373; DOI=10.1074/jbc.M104726200;
Byron K.L., Lucchesi P.A.;
"Signal transduction of physiological concentrations of vasopressin in
A7r5 vascular smooth muscle cells. A role for PYK2 and tyrosine
phosphorylation of K+ channels in the stimulation of Ca2+ spiking.";
J. Biol. Chem. 277:7298-7307(2002).
[10]
FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF NMDA RECEPTORS AND
REGULATION OF NMDA RECEPTOR CHANNEL ACTIVITY.
PubMed=12097497;
Heidinger V., Manzerra P., Wang X.Q., Strasser U., Yu S.P., Choi D.W.,
Behrens M.M.;
"Metabotropic glutamate receptor 1-induced upregulation of NMDA
receptor current: mediation through the Pyk2/Src-family kinase pathway
in cortical neurons.";
J. Neurosci. 22:5452-5461(2002).
[11]
FUNCTION, PHOSPHORYLATION AT TYR-402 AND TYR-580, AND CATALYTIC
ACTIVITY.
PubMed=16574377; DOI=10.1016/j.cellsig.2006.02.013;
Wu S.S., Jacamo R.O., Vong S.K., Rozengurt E.;
"Differential regulation of Pyk2 phosphorylation at Tyr-402 and Tyr-
580 in intestinal epithelial cells: roles of calcium, Src, Rho kinase,
and the cytoskeleton.";
Cell. Signal. 18:1932-1940(2006).
[12]
AUTOPHOSPHORYLATION, AND INTERACTION WITH DLG4.
PubMed=20071509; DOI=10.1523/JNEUROSCI.4992-08.2010;
Bartos J.A., Ulrich J.D., Li H., Beazely M.A., Chen Y.,
Macdonald J.F., Hell J.W.;
"Postsynaptic clustering and activation of Pyk2 by PSD-95.";
J. Neurosci. 30:449-463(2010).
[13]
FUNCTION.
PubMed=21451101; DOI=10.1152/ajpcell.00315.2010;
Perez J., Torres R.A., Rocic P., Cismowski M.J., Weber D.S.,
Darley-Usmar V.M., Lucchesi P.A.;
"PYK2 signaling is required for PDGF-dependent vascular smooth muscle
cell proliferation.";
Am. J. Physiol. 301:C242-C251(2011).
[14]
PHOSPHORYLATION AT TYR-402; TYR-579 AND TYR-580, AND SUBUNIT.
PubMed=20849950; DOI=10.1016/j.cellsig.2010.09.015;
Riggs D., Yang Z., Kloss J., Loftus J.C.;
"The Pyk2 FERM regulates Pyk2 complex formation and phosphorylation.";
Cell. Signal. 23:288-296(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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:7544443}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:16574377}.
-!- ENZYME 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer, or homooligomer. Interacts with NPHP1, ASAP1,
ASAP2, ARHGAP26, SKAP2 and TGFB1I1. The Tyr-402 phosphorylated
form interacts with SRC (via SH2 domain) and SRC family members.
Forms a signaling complex with EPHA1, LCK and phosphatidylinositol
3-kinase; upon activation by EFNA1. Interacts with GRB2 (via SH2
domain). Interacts with P53/TP53 and MDM2. Interacts with MYLK.
Interacts with BCAR1. Interacts with RB1CC1. Interacts with RHOU.
Interacts with VAV1. Interacts with PDPK1. Interacts with LPXN and
PTPN12 (By similarity). Interacts with SIRPA and SH2D3C. Interacts
(hypophosphorylated) with PXN. Interacts with ARHGAP10. Interacts
with KCNA2 (PubMed:11739373). {ECO:0000250,
ECO:0000269|PubMed:11739373, ECO:0000269|PubMed:20071509,
ECO:0000269|PubMed:20849950, ECO:0000269|PubMed:8849729,
ECO:0000269|PubMed:9422762}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9645946}.
Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane
{ECO:0000269|PubMed:9645946}; Peripheral membrane protein
{ECO:0000269|PubMed:9645946}; Cytoplasmic side
{ECO:0000269|PubMed:9645946}. Cell projection, lamellipodium
{ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Colocalizes with integrins at the cell
periphery. 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell junction, focal adhesion.
Note=Localizes to focal adhesions, but not isoform 1 and isoform
3.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P70600-1; Sequence=Displayed;
Name=2; Synonyms=PRNK;
IsoId=P70600-2; Sequence=VSP_004982, VSP_004983;
Name=3; Synonyms=PYK2s;
IsoId=P70600-3; Sequence=VSP_004984;
-!- TISSUE SPECIFICITY: Highly expressed in pulmonary vein endothelial
cells, lung and brain (at protein level). Isoform 1 is expressed
at high levels in the brain (hippocampus, cerebral cortex and
olfactory bulb) and poorly in the spleen and other tissues,
whereas isoforms 2 and 3 are expressed in the spleen and brain
(highest in cerebellum). {ECO:0000269|PubMed:11739395}.
-!- 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}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U69109; AAC52895.1; -; mRNA.
EMBL; D45854; BAA08290.1; -; mRNA.
EMBL; AF063890; AAC28340.1; -; mRNA.
EMBL; BC101921; AAI01922.1; -; mRNA.
PIR; A57434; A57434.
RefSeq; NP_059014.2; NM_017318.2. [P70600-1]
RefSeq; XP_006252205.1; XM_006252143.3. [P70600-1]
RefSeq; XP_006252206.1; XM_006252144.3. [P70600-1]
RefSeq; XP_006252207.1; XM_006252145.3. [P70600-3]
RefSeq; XP_008768995.1; XM_008770773.2. [P70600-1]
RefSeq; XP_008768996.1; XM_008770774.2. [P70600-1]
UniGene; Rn.11025; -.
ProteinModelPortal; P70600; -.
SMR; P70600; -.
BioGrid; 248405; 4.
CORUM; P70600; -.
MINT; MINT-266266; -.
STRING; 10116.ENSRNOP00000031615; -.
ChEMBL; CHEMBL1075222; -.
iPTMnet; P70600; -.
PhosphoSitePlus; P70600; -.
PaxDb; P70600; -.
PRIDE; P70600; -.
Ensembl; ENSRNOT00000030007; ENSRNOP00000031615; ENSRNOG00000027839. [P70600-1]
Ensembl; ENSRNOT00000030036; ENSRNOP00000036813; ENSRNOG00000027839. [P70600-1]
GeneID; 50646; -.
KEGG; rno:50646; -.
UCSC; RGD:628758; rat. [P70600-1]
CTD; 2185; -.
RGD; 628758; Ptk2b.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000069938; -.
HOVERGEN; HBG004018; -.
InParanoid; P70600; -.
KO; K05871; -.
OMA; QMLTASH; -.
OrthoDB; EOG091G03BN; -.
PhylomeDB; P70600; -.
TreeFam; TF316643; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-391160; Signal regulatory protein family interactions.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-451927; Interleukin-2 family signaling.
PRO; PR:P70600; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000027839; -.
Genevisible; P70600; RN.
GO; GO:0097440; C:apical dendrite; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0044297; C:cell body; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005938; C:cell cortex; IDA:RGD.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0030425; C:dendrite; IDA:Alzheimers_University_of_Toronto.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:Alzheimers_University_of_Toronto.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:Alzheimers_University_of_Toronto.
GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:Alzheimers_University_of_Toronto.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0007015; P:actin filament organization; IMP:RGD.
GO; GO:0090630; P:activation of GTPase activity; IMP:RGD.
GO; GO:0042976; P:activation of Janus kinase activity; IMP:RGD.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; IMP:RGD.
GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:RGD.
GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:RGD.
GO; GO:0030154; P:cell differentiation; IEP:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006968; P:cellular defense response; IMP:Alzheimers_University_of_Toronto.
GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:RGD.
GO; GO:0048041; P:focal adhesion assembly; IMP:RGD.
GO; GO:0014009; P:glial cell proliferation; IEP:RGD.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IMP:Alzheimers_University_of_Toronto.
GO; GO:0060292; P:long term synaptic depression; IMP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:Alzheimers_University_of_Toronto.
GO; GO:0000165; P:MAPK cascade; IMP:RGD.
GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IMP:RGD.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:Alzheimers_University_of_Toronto.
GO; GO:0030279; P:negative regulation of ossification; IMP:RGD.
GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IMP:RGD.
GO; GO:0001556; P:oocyte maturation; IMP:RGD.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:RGD.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:2000538; P:positive regulation of B cell chemotaxis; ISS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IEP:RGD.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:RGD.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:Alzheimers_University_of_Toronto.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:Alzheimers_University_of_Toronto.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0030826; P:regulation of cGMP biosynthetic process; IEA:Ensembl.
GO; GO:0010752; P:regulation of cGMP-mediated signaling; IEA:Ensembl.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:0032960; P:regulation of inositol trisphosphate biosynthetic process; ISS:UniProtKB.
GO; GO:0010758; P:regulation of macrophage chemotaxis; ISS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IPI:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
GO; GO:0000302; P:response to reactive oxygen species; IEP:RGD.
GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0043149; P:stress fiber assembly; IMP:RGD.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
InterPro; IPR005189; Focal_adhesion_kin_target_dom.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR030610; PTK2B.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR24418:SF94; PTHR24418:SF94; 1.
Pfam; PF00373; FERM_M; 1.
Pfam; PF03623; Focal_AT; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
ProDom; PD006413; Focal_adhesion_target_reg; 1.
SMART; SM00295; B41; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF68993; SSF68993; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Angiogenesis; ATP-binding;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Direct protein sequencing; Immunity; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Tyrosine-protein kinase.
CHAIN 1 1009 Protein-tyrosine kinase 2-beta.
/FTId=PRO_0000088083.
DOMAIN 39 359 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 425 683 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 431 439 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 503 509 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 801 1009 Interaction with TGFB1I1.
{ECO:0000269|PubMed:9422762}.
REGION 868 1009 Focal adhesion targeting (FAT).
COMPBIAS 701 767 Pro-rich.
COMPBIAS 831 869 Pro-rich.
ACT_SITE 549 549 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 457 457 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 402 402 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16574377,
ECO:0000269|PubMed:20849950}.
MOD_RES 579 579 Phosphotyrosine; by SRC, LYN and LCK.
{ECO:0000269|PubMed:20849950}.
MOD_RES 580 580 Phosphotyrosine; by SRC, LYN and LCK.
{ECO:0000269|PubMed:16574377,
ECO:0000269|PubMed:20849950}.
MOD_RES 722 722 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 765 765 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 834 834 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 839 839 Phosphoserine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 842 842 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 849 849 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 881 881 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14289}.
VAR_SEQ 1 771 Missing (in isoform 2).
{ECO:0000303|PubMed:9645946}.
/FTId=VSP_004982.
VAR_SEQ 739 780 Missing (in isoform 3).
{ECO:0000303|PubMed:9645946}.
/FTId=VSP_004984.
VAR_SEQ 772 780 NVFKRHSMR -> MGLIVLSSQ (in isoform 2).
{ECO:0000303|PubMed:9645946}.
/FTId=VSP_004983.
CONFLICT 205 205 E -> A (in Ref. 2; BAA08290).
{ECO:0000305}.
CONFLICT 807 807 V -> F (in Ref. 3; AAC28340).
{ECO:0000305}.
SEQUENCE 1009 AA; 115784 MW; D435A475BCA49E9B CRC64;
MSGVSEPLSR VKVGTLRPPE GPPEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK
CTVQTEIQEI ITSILLSGRI GPNIQLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC
LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC
LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS
LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDTKPTCLA
EFKQIRSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG YCRLQGEHKG
SLIIHAKKDG EKRNSLPQIP TLNLESRRSH LSESCSIESD IYAEIPDETL RRPGGPQYGV
AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN
LDHPHIVKLI GIIEEEPTWI VMELYPYGEL GHYLERNKNS LKVPTLVLYA LQICKAMAYL
ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPELC PPVLYTLMTR
CWDYDPSDRP RFTELVCSLS DIYQMERDIA IEQERNARYR PPKILEPTAF QEPPPKPSRP
KYKHPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR
EEDFIRPSSR EEAQQLWEAE KIKMRQVLDR QQKQMVEDSQ WLRREERCLD PMVYMNDKSP
LTPEKEAGYT EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLSQ
LPPEEYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL AELINKMRLA
QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV ANLAHPPAE


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