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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) (Related adhesion focal tyrosine kinase) (RAFTK)

 FAK2_MOUSE              Reviewed;        1009 AA.
Q9QVP9; B2RQ16; G3X8V1;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 174.
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;
AltName: Full=Related adhesion focal tyrosine kinase;
Short=RAFTK;
Name=Ptk2b; Synonyms=Fak2, Pyk2, Raftk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7499242; DOI=10.1074/jbc.270.46.27742;
Avraham S., London R., Fu Y., Ota S., Hiregowdara D., Li J., Jiang S.,
Pasztor L.M., White R.A., Groopman J.E., Avraham H.;
"Identification and characterization of a novel related adhesion focal
tyrosine kinase (RAFTK) from megakaryocytes and brain.";
J. Biol. Chem. 270:27742-27751(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
PROTEIN SEQUENCE OF 469-479, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
INTERACTION WITH PXN.
PubMed=8940124; DOI=10.1074/jbc.271.49.31222;
Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A.,
Sattler M., Avraham H., Griffin J.D.;
"The related adhesion focal tyrosine kinase forms a complex with
paxillin in hematopoietic cells.";
J. Biol. Chem. 271:31222-31226(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]
INTERACTION WITH SIRPA.
PubMed=10469599; DOI=10.1016/S0960-9822(99)80401-1;
Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
Schraven B., Neel B.G.;
"SHPS-1 is a scaffold for assembling distinct adhesion-regulated
multi-protein complexes in macrophages.";
Curr. Biol. 9:927-930(1999).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION IN B-CELL DIFFERENTIATION; B-CELL
CHEMOTAXIS AND IMMUNE RESPONSE.
PubMed=10881171; DOI=10.1038/76882;
Guinamard R., Okigaki M., Schlessinger J., Ravetch J.V.;
"Absence of marginal zone B cells in Pyk-2-deficient mice defines
their role in the humoral response.";
Nat. Immunol. 1:31-36(2000).
[10]
INTERACTION WITH ARHGAP10, AND FUNCTION IN REGULATION OF ARHGAP10
ACTIVITY AND ACTIVATION OF CDC42 AND RHOA.
PubMed=11238453; DOI=10.1083/jcb.152.5.971;
Ren X.-R., Du Q.-S., Huang Y.-Z., Ao S.-Z., Mei L., Xiong W.-C.;
"Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2
interacting with PSGAP, a novel pleckstrin homology and Src homology 3
domain containing rhoGAP protein.";
J. Cell Biol. 152:971-984(2001).
[11]
PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
PubMed=11420674; DOI=10.1038/sj.onc.1204359;
Nakamura K., Yano H., Schaefer E., Sabe H.;
"Different modes and qualities of tyrosine phosphorylation of Fak and
Pyk2 during epithelial-mesenchymal transdifferentiation and cell
migration: analysis of specific phosphorylation events using site-
directed antibodies.";
Oncogene 20:2626-2635(2001).
[12]
PHOSPHORYLATION AT TYR-402, AND INTERACTION WITH NPHP1.
PubMed=11493697; DOI=10.1073/pnas.171269898;
Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.;
"Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers
phosphorylation of Pyk2.";
Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001).
[13]
INTERACTION WITH SH2D3C.
PubMed=12486027; DOI=10.1074/jbc.M207942200;
Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
"A novel hematopoietic adaptor protein, Chat-H, positively regulates T
cell receptor-mediated interleukin-2 production by Jurkat cells.";
J. Biol. Chem. 278:6012-6017(2003).
[14]
INTERACTION WITH LPXN AMD PTPN12.
PubMed=12674328; DOI=10.1359/jbmr.2003.18.4.669;
Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y.,
Goldknopf J., Hruska K.A.;
"Leupaxin is a critical adaptor protein in the adhesion zone of the
osteoclast.";
J. Bone Miner. Res. 18:669-685(2003).
[15]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12960403; DOI=10.1073/pnas.1834348100;
Okigaki M., Davis C., Falasca M., Harroch S., Felsenfeld D.P.,
Sheetz M.P., Schlessinger J.;
"Pyk2 regulates multiple signaling events crucial for macrophage
morphology and migration.";
Proc. Natl. Acad. Sci. U.S.A. 100:10740-10745(2003).
[16]
FUNCTION IN BONE RESORPTION, INTERACTION WITH SRC, PHOSPHORYLATION AT
TYR-402, AND MUTAGENESIS OF TYR-402.
PubMed=14739300; DOI=10.1074/jbc.M311032200;
Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.;
"Src kinase activity is essential for osteoclast function.";
J. Biol. Chem. 279:17660-17666(2004).
[17]
PHOSPHORYLATION IN RESPONSE TO FGR.
PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
Lowell C.A., Berton G.;
"The proto-oncogene Fgr regulates cell migration and this requires its
plasma membrane localization.";
Exp. Cell Res. 302:253-269(2005).
[18]
FUNCTION IN VEGFA SIGNALING; REGULATION OF INTRACELLULAR CALCIUM
LEVELS; ACTIVATION OF AKT1 AND RAC1; PHOSPHORYLATION OF SRC;
REORGANIZATION OF ACTIN CYTOSKELETON; CELL MIGRATION AND ANGIOGENESIS,
AND INTERACTION WITH SRC.
PubMed=17698736; DOI=10.1161/CIRCULATIONAHA.106.645416;
Matsui A., Okigaki M., Amano K., Adachi Y., Jin D., Takai S.,
Yamashita T., Kawashima S., Kurihara T., Miyazaki M., Tateishi K.,
Matsunaga S., Katsume A., Honshou S., Takahashi T., Matoba S.,
Kusaba T., Tatsumi T., Matsubara H.;
"Central role of calcium-dependent tyrosine kinase PYK2 in endothelial
nitric oxide synthase-mediated angiogenic response and vascular
function.";
Circulation 116:1041-1051(2007).
[19]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17846174; DOI=10.1083/jcb.200701148;
Gil-Henn H., Destaing O., Sims N.A., Aoki K., Alles N., Neff L.,
Sanjay A., Bruzzaniti A., De Camilli P., Baron R., Schlessinger J.;
"Defective microtubule-dependent podosome organization in osteoclasts
leads to increased bone density in Pyk2(-/-) mice.";
J. Cell Biol. 178:1053-1064(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; TYR-579 AND
TYR-580, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[21]
DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=17537919; DOI=10.1073/pnas.0701421104;
Buckbinder L., Crawford D.T., Qi H., Ke H.Z., Olson L.M., Long K.R.,
Bonnette P.C., Baumann A.P., Hambor J.E., Grasser W.A. III, Pan L.C.,
Owen T.A., Luzzio M.J., Hulford C.A., Gebhard D.F., Paralkar V.M.,
Simmons H.A., Kath J.C., Roberts W.G., Smock S.L., Guzman-Perez A.,
Brown T.A., Li M.;
"Proline-rich tyrosine kinase 2 regulates osteoprogenitor cells and
bone formation, and offers an anabolic treatment approach for
osteoporosis.";
Proc. Natl. Acad. Sci. U.S.A. 104:10619-10624(2007).
[22]
FUNCTION DURING LUNG INJURY, PHOSPHORYLATION BY MYLK, AND INTERACTION
WITH MYLK.
PubMed=18587400; DOI=10.1038/ni.1628;
Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.;
"Nonmuscle myosin light-chain kinase mediates neutrophil
transmigration in sepsis-induced lung inflammation by activating beta2
integrins.";
Nat. Immunol. 9:880-886(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[24]
FUNCTION.
PubMed=19561089; DOI=10.1074/jbc.M109.013169;
Tse K.W., Dang-Lawson M., Lee R.L., Vong D., Bulic A., Buckbinder L.,
Gold M.R.;
"B cell receptor-induced phosphorylation of Pyk2 and focal adhesion
kinase involves integrins and the Rap GTPases and is required for B
cell spreading.";
J. Biol. Chem. 284:22865-22877(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[26]
FUNCTION IN CELL PROLIFERATION AND REGULATION OF P53/TP53
UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=19880522; DOI=10.1074/jbc.M109.064212;
Lim S.T., Miller N.L., Nam J.O., Chen X.L., Lim Y., Schlaepfer D.D.;
"Pyk2 inhibition of p53 as an adaptive and intrinsic mechanism
facilitating cell proliferation and survival.";
J. Biol. Chem. 285:1743-1753(2010).
[27]
FUNCTION, PHOSPHORYLATION AT TYR-402 AND TYR-579, AND ENZYME
REGULATION.
PubMed=20688918; DOI=10.1074/jbc.M110.118265;
Lysechko T.L., Cheung S.M., Ostergaard H.L.;
"Regulation of the tyrosine kinase Pyk2 by calcium is through
production of reactive oxygen species in cytotoxic T lymphocytes.";
J. Biol. Chem. 285:31174-31184(2010).
[28]
INTERACTION WITH PXN, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
TYR-402; TYR-580 AND TYR-881.
PubMed=21195757; DOI=10.1016/j.cellsig.2010.12.006;
St-Pierre J., Lysechko T.L., Ostergaard H.L.;
"Hypophosphorylated and inactive Pyk2 associates with paxillin at the
microtubule organizing center in hematopoietic cells.";
Cell. Signal. 23:718-730(2011).
[29]
FUNCTION IN SPROUTING ANGIOGENESIS.
PubMed=21640103; DOI=10.1016/j.yexcr.2011.05.006;
Shen C.J., Raghavan S., Xu Z., Baranski J.D., Yu X., Wozniak M.A.,
Miller J.S., Gupta M., Buckbinder L., Chen C.S.;
"Decreased cell adhesion promotes angiogenesis in a Pyk2-dependent
manner.";
Exp. Cell Res. 317:1860-1871(2011).
-!- 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}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:17537919}.
-!- 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. {ECO:0000269|PubMed:17537919,
ECO:0000269|PubMed:20688918}.
-!- SUBUNIT: Homodimer, or homooligomer. Interacts with KCNA2 (By
similarity). 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 DLG4. Interacts with LPXN and
PTPN12. Interacts with SIRPA and SH2D3C. Interacts
(hypophosphorylated) with PXN. Interacts with ARHGAP10.
{ECO:0000250|UniProtKB:P70600, ECO:0000269|PubMed:10469599,
ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:11493697,
ECO:0000269|PubMed:12486027, ECO:0000269|PubMed:12674328,
ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:17698736,
ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:21195757,
ECO:0000269|PubMed:8940124, ECO:0000269|PubMed:9422762}.
-!- 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}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate, appear normal and are fertile. Mice display increased bone
formation and high bone mass, due to defects in osteoclastic bone
resorption. Osteoclasts display defects in actin cytoskeleton
reorganization, plus altered Rho activity, microtubule
stabilization and podosome organization. Mice also display
increased differentiation and activity of osteoprogenitor cells.
Macrophages from mutant mice display defects in their responses to
chemokines, including defects in cell polarization, actin
cytoskeleton reorganization, directed migration towards sites of
inflammation, but also defects in the regulation of intracellular
Ca(2+) levels, phosphatidylinositol 3-kinase activity and inositol
1,4,5-trisphosphate production. Mutant mice have normal B-cell
polulations in bone marrow, lymph nodes and blood, but lack
marginal zone B-cells in the spleen. {ECO:0000269|PubMed:10881171,
ECO:0000269|PubMed:12960403, ECO:0000269|PubMed:17537919,
ECO:0000269|PubMed:17846174}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AC126272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466535; EDL36001.1; -; Genomic_DNA.
EMBL; BC137704; AAI37705.1; -; mRNA.
EMBL; BC144849; AAI44850.1; -; mRNA.
CCDS; CCDS49526.1; -.
RefSeq; NP_001155838.1; NM_001162366.1.
RefSeq; XP_006518789.1; XM_006518726.3.
RefSeq; XP_011243296.1; XM_011244994.2.
UniGene; Mm.21613; -.
ProteinModelPortal; Q9QVP9; -.
SMR; Q9QVP9; -.
BioGrid; 202467; 12.
CORUM; Q9QVP9; -.
IntAct; Q9QVP9; 5.
MINT; MINT-266339; -.
STRING; 10090.ENSMUSP00000022622; -.
BindingDB; Q9QVP9; -.
ChEMBL; CHEMBL1075289; -.
iPTMnet; Q9QVP9; -.
PhosphoSitePlus; Q9QVP9; -.
EPD; Q9QVP9; -.
MaxQB; Q9QVP9; -.
PaxDb; Q9QVP9; -.
PRIDE; Q9QVP9; -.
Ensembl; ENSMUST00000022622; ENSMUSP00000022622; ENSMUSG00000059456.
Ensembl; ENSMUST00000178730; ENSMUSP00000137008; ENSMUSG00000059456.
GeneID; 19229; -.
KEGG; mmu:19229; -.
UCSC; uc011znr.1; mouse.
CTD; 2185; -.
MGI; MGI:104908; Ptk2b.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000069938; -.
HOVERGEN; HBG004018; -.
InParanoid; Q9QVP9; -.
KO; K05871; -.
OMA; QMLTASH; -.
OrthoDB; EOG091G03BN; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-391160; Signal regulatory protein family interactions.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-451927; Interleukin-2 family signaling.
PRO; PR:Q9QVP9; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000059456; -.
CleanEx; MM_PTK2B; -.
ExpressionAtlas; Q9QVP9; baseline and differential.
Genevisible; Q9QVP9; MM.
GO; GO:0097440; C:apical dendrite; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0044297; C:cell body; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0030425; C:dendrite; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0030426; C:growth cone; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; ISS:Alzheimers_University_of_Toronto.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:Alzheimers_University_of_Toronto.
GO; GO:0004972; F:NMDA glutamate receptor activity; IEA:Ensembl.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
GO; GO:0042976; P:activation of Janus kinase activity; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:0045453; P:bone resorption; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006968; P:cellular defense response; ISS:Alzheimers_University_of_Toronto.
GO; GO:0071498; P:cellular response to fluid shear stress; IMP:MGI.
GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
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; ISS:Alzheimers_University_of_Toronto.
GO; GO:0060292; P:long term synaptic depression; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030502; P:negative regulation of bone mineralization; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:MGI.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:2000538; P:positive regulation of B cell chemotaxis; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS: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; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0030826; P:regulation of cGMP biosynthetic process; IMP:UniProtKB.
GO; GO:0010752; P:regulation of cGMP-mediated signaling; IMP:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
GO; GO:0032960; P:regulation of inositol trisphosphate biosynthetic process; IMP:UniProtKB.
GO; GO:0010758; P:regulation of macrophage chemotaxis; IMP:UniProtKB.
GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000058; P:regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:UniProtKB.
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; 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_0000088082.
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:0000250}.
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:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000250|UniProtKB:Q14289}.
MOD_RES 402 402 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:11493697,
ECO:0000269|PubMed:14739300,
ECO:0000269|PubMed:20688918,
ECO:0000269|PubMed:21195757}.
MOD_RES 579 579 Phosphotyrosine; by SRC, LYN and LCK.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:20688918}.
MOD_RES 580 580 Phosphotyrosine; by SRC, LYN and LCK.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:21195757}.
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:0000269|PubMed:11420674,
ECO:0000269|PubMed:21195757}.
MUTAGEN 402 402 Y->A: Loss of phosphorylation and
interaction with SRC, and inhibition of
bone resorption.
{ECO:0000269|PubMed:14739300}.
CONFLICT 306 306 K -> R (in Ref. 4; AAI37705/AAI44850).
{ECO:0000305}.
SEQUENCE 1009 AA; 115794 MW; A17C858ECC9990E9 CRC64;
MSGVSEPLSR VKVGTLRRPE 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
EFKQIKSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG YCRLQGEHKG
SLIMHAKKDG EKRNSLPQIP TLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGV
AREEVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTQDNKEK FMSEAVIMKN
LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVPTLVLYT LQICKAMAYL
ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPELC PPVLYTLMTR
CWDYDPSDRP RFTELVCSLS DIYQMEKDIA IEQERNARYR PPKILEPTTF QEPPPKPSRP
KYRPPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR
EEDFIRPSSR EEAQQLWEAE KIKMKQVLER QQKQMVEDSQ WLRREERCLD PMVYMNDKSP
LTPEKEAGYT EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLGQ
LPPEDYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL AELINKMKLA
QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV ANLAHPPAE


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