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FAK2_MOUSE
ID   FAK2_MOUSE              Reviewed;        1009 AA.
AC   Q9QVP9; B2RQ16; G3X8V1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 208.
DE   RecName: Full=Protein-tyrosine kinase 2-beta;
DE            EC=2.7.10.2;
DE   AltName: Full=Calcium-dependent tyrosine kinase;
DE            Short=CADTK;
DE   AltName: Full=Calcium-regulated non-receptor proline-rich tyrosine kinase;
DE   AltName: Full=Cell adhesion kinase beta;
DE            Short=CAK-beta;
DE            Short=CAKB;
DE   AltName: Full=Focal adhesion kinase 2;
DE            Short=FADK 2;
DE   AltName: Full=Proline-rich tyrosine kinase 2;
DE   AltName: Full=Related adhesion focal tyrosine kinase;
DE            Short=RAFTK;
GN   Name=Ptk2b; Synonyms=Fak2, Pyk2, Raftk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7499242; DOI=10.1074/jbc.270.46.27742;
RA   Avraham S., London R., Fu Y., Ota S., Hiregowdara D., Li J., Jiang S.,
RA   Pasztor L.M., White R.A., Groopman J.E., Avraham H.;
RT   "Identification and characterization of a novel related adhesion focal
RT   tyrosine kinase (RAFTK) from megakaryocytes and brain.";
RL   J. Biol. Chem. 270:27742-27751(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 469-479, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   INTERACTION WITH PXN.
RX   PubMed=8940124; DOI=10.1074/jbc.271.49.31222;
RA   Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A.,
RA   Sattler M., Avraham H., Griffin J.D.;
RT   "The related adhesion focal tyrosine kinase forms a complex with paxillin
RT   in hematopoietic cells.";
RL   J. Biol. Chem. 271:31222-31226(1996).
RN   [7]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=9422762; DOI=10.1074/jbc.273.2.1003;
RA   Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M.,
RA   Takahashi S., Suzuki R., Sasaki T.;
RT   "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of
RT   proteins localized at focal adhesions.";
RL   J. Biol. Chem. 273:1003-1014(1998).
RN   [8]
RP   INTERACTION WITH SIRPA.
RX   PubMed=10469599; DOI=10.1016/s0960-9822(99)80401-1;
RA   Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
RA   Schraven B., Neel B.G.;
RT   "SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-
RT   protein complexes in macrophages.";
RL   Curr. Biol. 9:927-930(1999).
RN   [9]
RP   DISRUPTION PHENOTYPE, AND FUNCTION IN B-CELL DIFFERENTIATION; B-CELL
RP   CHEMOTAXIS AND IMMUNE RESPONSE.
RX   PubMed=10881171; DOI=10.1038/76882;
RA   Guinamard R., Okigaki M., Schlessinger J., Ravetch J.V.;
RT   "Absence of marginal zone B cells in Pyk-2-deficient mice defines their
RT   role in the humoral response.";
RL   Nat. Immunol. 1:31-36(2000).
RN   [10]
RP   INTERACTION WITH ARHGAP10, AND FUNCTION IN REGULATION OF ARHGAP10 ACTIVITY
RP   AND ACTIVATION OF CDC42 AND RHOA.
RX   PubMed=11238453; DOI=10.1083/jcb.152.5.971;
RA   Ren X.-R., Du Q.-S., Huang Y.-Z., Ao S.-Z., Mei L., Xiong W.-C.;
RT   "Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting
RT   with PSGAP, a novel pleckstrin homology and Src homology 3 domain
RT   containing rhoGAP protein.";
RL   J. Cell Biol. 152:971-984(2001).
RN   [11]
RP   PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
RX   PubMed=11420674; DOI=10.1038/sj.onc.1204359;
RA   Nakamura K., Yano H., Schaefer E., Sabe H.;
RT   "Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2
RT   during epithelial-mesenchymal transdifferentiation and cell migration:
RT   analysis of specific phosphorylation events using site-directed
RT   antibodies.";
RL   Oncogene 20:2626-2635(2001).
RN   [12]
RP   PHOSPHORYLATION AT TYR-402, AND INTERACTION WITH NPHP1.
RX   PubMed=11493697; DOI=10.1073/pnas.171269898;
RA   Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.;
RT   "Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers
RT   phosphorylation of Pyk2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001).
RN   [13]
RP   INTERACTION WITH SH2D3C.
RX   PubMed=12486027; DOI=10.1074/jbc.m207942200;
RA   Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
RT   "A novel hematopoietic adaptor protein, Chat-H, positively regulates T cell
RT   receptor-mediated interleukin-2 production by Jurkat cells.";
RL   J. Biol. Chem. 278:6012-6017(2003).
RN   [14]
RP   INTERACTION WITH LPXN AMD PTPN12.
RX   PubMed=12674328; DOI=10.1359/jbmr.2003.18.4.669;
RA   Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y.,
RA   Goldknopf J., Hruska K.A.;
RT   "Leupaxin is a critical adaptor protein in the adhesion zone of the
RT   osteoclast.";
RL   J. Bone Miner. Res. 18:669-685(2003).
RN   [15]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12960403; DOI=10.1073/pnas.1834348100;
RA   Okigaki M., Davis C., Falasca M., Harroch S., Felsenfeld D.P., Sheetz M.P.,
RA   Schlessinger J.;
RT   "Pyk2 regulates multiple signaling events crucial for macrophage morphology
RT   and migration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10740-10745(2003).
RN   [16]
RP   FUNCTION IN BONE RESORPTION, INTERACTION WITH SRC, PHOSPHORYLATION AT
RP   TYR-402, AND MUTAGENESIS OF TYR-402.
RX   PubMed=14739300; DOI=10.1074/jbc.m311032200;
RA   Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.;
RT   "Src kinase activity is essential for osteoclast function.";
RL   J. Biol. Chem. 279:17660-17666(2004).
RN   [17]
RP   PHOSPHORYLATION IN RESPONSE TO FGR.
RX   PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
RA   Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
RA   Lowell C.A., Berton G.;
RT   "The proto-oncogene Fgr regulates cell migration and this requires its
RT   plasma membrane localization.";
RL   Exp. Cell Res. 302:253-269(2005).
RN   [18]
RP   FUNCTION IN VEGFA SIGNALING; REGULATION OF INTRACELLULAR CALCIUM LEVELS;
RP   ACTIVATION OF AKT1 AND RAC1; PHOSPHORYLATION OF SRC; REORGANIZATION OF
RP   ACTIN CYTOSKELETON; CELL MIGRATION AND ANGIOGENESIS, AND INTERACTION WITH
RP   SRC.
RX   PubMed=17698736; DOI=10.1161/circulationaha.106.645416;
RA   Matsui A., Okigaki M., Amano K., Adachi Y., Jin D., Takai S., Yamashita T.,
RA   Kawashima S., Kurihara T., Miyazaki M., Tateishi K., Matsunaga S.,
RA   Katsume A., Honshou S., Takahashi T., Matoba S., Kusaba T., Tatsumi T.,
RA   Matsubara H.;
RT   "Central role of calcium-dependent tyrosine kinase PYK2 in endothelial
RT   nitric oxide synthase-mediated angiogenic response and vascular function.";
RL   Circulation 116:1041-1051(2007).
RN   [19]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17846174; DOI=10.1083/jcb.200701148;
RA   Gil-Henn H., Destaing O., Sims N.A., Aoki K., Alles N., Neff L., Sanjay A.,
RA   Bruzzaniti A., De Camilli P., Baron R., Schlessinger J.;
RT   "Defective microtubule-dependent podosome organization in osteoclasts leads
RT   to increased bone density in Pyk2(-/-) mice.";
RL   J. Cell Biol. 178:1053-1064(2007).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; TYR-579 AND TYR-580, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [21]
RP   DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP   REGULATION.
RX   PubMed=17537919; DOI=10.1073/pnas.0701421104;
RA   Buckbinder L., Crawford D.T., Qi H., Ke H.Z., Olson L.M., Long K.R.,
RA   Bonnette P.C., Baumann A.P., Hambor J.E., Grasser W.A. III, Pan L.C.,
RA   Owen T.A., Luzzio M.J., Hulford C.A., Gebhard D.F., Paralkar V.M.,
RA   Simmons H.A., Kath J.C., Roberts W.G., Smock S.L., Guzman-Perez A.,
RA   Brown T.A., Li M.;
RT   "Proline-rich tyrosine kinase 2 regulates osteoprogenitor cells and bone
RT   formation, and offers an anabolic treatment approach for osteoporosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10619-10624(2007).
RN   [22]
RP   FUNCTION DURING LUNG INJURY, PHOSPHORYLATION BY MYLK, AND INTERACTION WITH
RP   MYLK.
RX   PubMed=18587400; DOI=10.1038/ni.1628;
RA   Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.;
RT   "Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in
RT   sepsis-induced lung inflammation by activating beta2 integrins.";
RL   Nat. Immunol. 9:880-886(2008).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [24]
RP   FUNCTION.
RX   PubMed=19561089; DOI=10.1074/jbc.m109.013169;
RA   Tse K.W., Dang-Lawson M., Lee R.L., Vong D., Bulic A., Buckbinder L.,
RA   Gold M.R.;
RT   "B cell receptor-induced phosphorylation of Pyk2 and focal adhesion kinase
RT   involves integrins and the Rap GTPases and is required for B cell
RT   spreading.";
RL   J. Biol. Chem. 284:22865-22877(2009).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [26]
RP   FUNCTION IN CELL PROLIFERATION AND REGULATION OF P53/TP53 UBIQUITINATION,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=19880522; DOI=10.1074/jbc.m109.064212;
RA   Lim S.T., Miller N.L., Nam J.O., Chen X.L., Lim Y., Schlaepfer D.D.;
RT   "Pyk2 inhibition of p53 as an adaptive and intrinsic mechanism facilitating
RT   cell proliferation and survival.";
RL   J. Biol. Chem. 285:1743-1753(2010).
RN   [27]
RP   FUNCTION, PHOSPHORYLATION AT TYR-402 AND TYR-579, AND ACTIVITY REGULATION.
RX   PubMed=20688918; DOI=10.1074/jbc.m110.118265;
RA   Lysechko T.L., Cheung S.M., Ostergaard H.L.;
RT   "Regulation of the tyrosine kinase Pyk2 by calcium is through production of
RT   reactive oxygen species in cytotoxic T lymphocytes.";
RL   J. Biol. Chem. 285:31174-31184(2010).
RN   [28]
RP   INTERACTION WITH PXN, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-402;
RP   TYR-580 AND TYR-881.
RX   PubMed=21195757; DOI=10.1016/j.cellsig.2010.12.006;
RA   St-Pierre J., Lysechko T.L., Ostergaard H.L.;
RT   "Hypophosphorylated and inactive Pyk2 associates with paxillin at the
RT   microtubule organizing center in hematopoietic cells.";
RL   Cell. Signal. 23:718-730(2011).
RN   [29]
RP   FUNCTION IN SPROUTING ANGIOGENESIS.
RX   PubMed=21640103; DOI=10.1016/j.yexcr.2011.05.006;
RA   Shen C.J., Raghavan S., Xu Z., Baranski J.D., Yu X., Wozniak M.A.,
RA   Miller J.S., Gupta M., Buckbinder L., Chen C.S.;
RT   "Decreased cell adhesion promotes angiogenesis in a Pyk2-dependent
RT   manner.";
RL   Exp. Cell Res. 317:1860-1871(2011).
CC   -!- FUNCTION: Non-receptor protein-tyrosine kinase that regulates
CC       reorganization of the actin cytoskeleton, cell polarization, cell
CC       migration, adhesion, spreading and bone remodeling. Plays a role in the
CC       regulation of the humoral immune response, and is required for normal
CC       levels of marginal B-cells in the spleen and normal migration of
CC       splenic B-cells. Required for normal macrophage polarization and
CC       migration towards sites of inflammation. Regulates cytoskeleton
CC       rearrangement and cell spreading in T-cells, and contributes to the
CC       regulation of T-cell responses. Promotes osteoclastic bone resorption;
CC       this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and
CC       activity of osteoprogenitor cells. Functions in signaling downstream of
CC       integrin and collagen receptors, immune receptors, G-protein coupled
CC       receptors (GPCR), cytokine, chemokine and growth factor receptors, and
CC       mediates responses to cellular stress. Forms multisubunit signaling
CC       complexes with SRC and SRC family members upon activation; this leads
CC       to the phosphorylation of additional tyrosine residues, creating
CC       binding sites for scaffold proteins, effectors and substrates.
CC       Regulates numerous signaling pathways. Promotes activation of
CC       phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.
CC       Promotes activation of NOS3. Regulates production of the cellular
CC       messenger cGMP. Promotes activation of the MAP kinase signaling
CC       cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1.
CC       Promotes activation of Rho family GTPases, such as RHOA and RAC1.
CC       Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and
CC       thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and
CC       proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and
CC       SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373',
CC       and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA
CC       receptors by SRC family members, and thereby contributes to the
CC       regulation of NMDA receptor ion channel activity and intracellular
CC       Ca(2+) levels. May also regulate potassium ion transport by
CC       phosphorylation of potassium channel subunits. Phosphorylates SRC; this
CC       increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and
CC       SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires
CC       both SRC and PTK2/PYK2 (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:10881171, ECO:0000269|PubMed:11238453,
CC       ECO:0000269|PubMed:12960403, ECO:0000269|PubMed:14739300,
CC       ECO:0000269|PubMed:17537919, ECO:0000269|PubMed:17698736,
CC       ECO:0000269|PubMed:17846174, ECO:0000269|PubMed:18587400,
CC       ECO:0000269|PubMed:19561089, ECO:0000269|PubMed:19880522,
CC       ECO:0000269|PubMed:20688918, ECO:0000269|PubMed:21640103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC         ECO:0000269|PubMed:17537919};
CC   -!- ACTIVITY REGULATION: Activated in response to stimuli that lead to
CC       increased intracellular Ca(2+) levels; this activation is indirect and
CC       may be mediated by calcium-mediated production of reactive oxygen
CC       species (ROS). Activated by autophosphorylation at Tyr-402; this
CC       creates a binding site for SRC family kinases and leads to
CC       phosphorylation at additional tyrosine residues. Phosphorylation at
CC       Tyr-402, Tyr-579 and Tyr-580 is required for optimal kinase activity.
CC       {ECO:0000269|PubMed:17537919, ECO:0000269|PubMed:20688918}.
CC   -!- SUBUNIT: Homodimer, or homooligomer. Interacts with KCNA2 (By
CC       similarity). Interacts with NPHP1, ASAP1, ASAP2, ARHGAP26, SKAP2 and
CC       TGFB1I1. The Tyr-402 phosphorylated form interacts with SRC (via SH2
CC       domain) and SRC family members. Forms a signaling complex with EPHA1,
CC       LCK and phosphatidylinositol 3-kinase; upon activation by EFNA1.
CC       Interacts with GRB2 (via SH2 domain). Interacts with P53/TP53 and MDM2.
CC       Interacts with MYLK. Interacts with BCAR1. Interacts with RB1CC1.
CC       Interacts with RHOU. Interacts with VAV1. Interacts with PDPK1.
CC       Interacts with DLG4. Interacts with LPXN and PTPN12. Interacts with
CC       SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts
CC       with ARHGAP10. {ECO:0000250|UniProtKB:P70600,
CC       ECO:0000269|PubMed:10469599, ECO:0000269|PubMed:11238453,
CC       ECO:0000269|PubMed:11493697, ECO:0000269|PubMed:12486027,
CC       ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:14739300,
CC       ECO:0000269|PubMed:17698736, ECO:0000269|PubMed:18587400,
CC       ECO:0000269|PubMed:21195757, ECO:0000269|PubMed:8940124,
CC       ECO:0000269|PubMed:9422762}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region
CC       {ECO:0000250}. Cell membrane; Peripheral membrane protein; Cytoplasmic
CC       side. Cell junction, focal adhesion. Cell projection, lamellipodium
CC       {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery
CC       (By similarity). Interaction with NPHP1 induces the membrane-
CC       association of the kinase. Colocalizes with PXN at the microtubule-
CC       organizing center. The tyrosine phosphorylated form is detected at
CC       cell-cell contacts. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to various stimuli
CC       that elevate the intracellular calcium concentration; this activation
CC       is indirect and may be mediated by production of reactive oxygen
CC       species (ROS). Tyr-402 is the major autophosphorylation site, but other
CC       kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in
CC       trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine
CC       residues on the other subunit. Phosphorylation at Tyr-402 promotes
CC       interaction with SRC and SRC family members, leading to phosphorylation
CC       at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is
CC       important for interaction with GRB2. Phosphorylated on tyrosine
CC       residues upon activation of FGR and PKC. Recruitment by NPHP1 to cell
CC       matrix adhesions initiates Tyr-402 phosphorylation. In monocytes,
CC       adherence to substrata is required for tyrosine phosphorylation and
CC       kinase activation. Angiotensin II, thapsigargin and L-alpha-
CC       lysophosphatidic acid (LPA) also induce autophosphorylation and
CC       increase kinase activity. Phosphorylation by MYLK promotes ITGB2
CC       activation and is thus essential to trigger neutrophil transmigration
CC       during lung injury. Dephosphorylated by PTPN12 (By similarity).
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate,
CC       appear normal and are fertile. Mice display increased bone formation
CC       and high bone mass, due to defects in osteoclastic bone resorption.
CC       Osteoclasts display defects in actin cytoskeleton reorganization, plus
CC       altered Rho activity, microtubule stabilization and podosome
CC       organization. Mice also display increased differentiation and activity
CC       of osteoprogenitor cells. Macrophages from mutant mice display defects
CC       in their responses to chemokines, including defects in cell
CC       polarization, actin cytoskeleton reorganization, directed migration
CC       towards sites of inflammation, but also defects in the regulation of
CC       intracellular Ca(2+) levels, phosphatidylinositol 3-kinase activity and
CC       inositol 1,4,5-trisphosphate production. Mutant mice have normal B-cell
CC       polulations in bone marrow, lymph nodes and blood, but lack marginal
CC       zone B-cells in the spleen. {ECO:0000269|PubMed:10881171,
CC       ECO:0000269|PubMed:12960403, ECO:0000269|PubMed:17537919,
CC       ECO:0000269|PubMed:17846174}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. FAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AC126272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466535; EDL36001.1; -; Genomic_DNA.
DR   EMBL; BC137704; AAI37705.1; -; mRNA.
DR   EMBL; BC144849; AAI44850.1; -; mRNA.
DR   CCDS; CCDS49526.1; -.
DR   RefSeq; NP_001155838.1; NM_001162366.1.
DR   RefSeq; XP_006518789.1; XM_006518726.3.
DR   RefSeq; XP_011243296.1; XM_011244994.2.
DR   AlphaFoldDB; Q9QVP9; -.
DR   SMR; Q9QVP9; -.
DR   BioGRID; 202467; 35.
DR   CORUM; Q9QVP9; -.
DR   IntAct; Q9QVP9; 6.
DR   MINT; Q9QVP9; -.
DR   STRING; 10090.ENSMUSP00000106750; -.
DR   BindingDB; Q9QVP9; -.
DR   ChEMBL; CHEMBL1075289; -.
DR   iPTMnet; Q9QVP9; -.
DR   PhosphoSitePlus; Q9QVP9; -.
DR   CPTAC; non-CPTAC-3644; -.
DR   EPD; Q9QVP9; -.
DR   jPOST; Q9QVP9; -.
DR   MaxQB; Q9QVP9; -.
DR   PaxDb; Q9QVP9; -.
DR   PRIDE; Q9QVP9; -.
DR   ProteomicsDB; 271727; -.
DR   Antibodypedia; 3551; 1056 antibodies from 44 providers.
DR   DNASU; 19229; -.
DR   Ensembl; ENSMUST00000022622; ENSMUSP00000022622; ENSMUSG00000059456.
DR   Ensembl; ENSMUST00000178730; ENSMUSP00000137008; ENSMUSG00000059456.
DR   GeneID; 19229; -.
DR   KEGG; mmu:19229; -.
DR   UCSC; uc011znr.1; mouse.
DR   CTD; 2185; -.
DR   MGI; MGI:104908; Ptk2b.
DR   VEuPathDB; HostDB:ENSMUSG00000059456; -.
DR   eggNOG; KOG4257; Eukaryota.
DR   GeneTree; ENSGT00940000157269; -.
DR   InParanoid; Q9QVP9; -.
DR   OMA; IMELYSY; -.
DR   OrthoDB; 43729at2759; -.
DR   PhylomeDB; Q9QVP9; -.
DR   BRENDA; 2.7.10.2; 3474.
DR   Reactome; R-MMU-391160; Signal regulatory protein family interactions.
DR   Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR   Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR   BioGRID-ORCS; 19229; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Ptk2b; mouse.
DR   PRO; PR:Q9QVP9; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9QVP9; protein.
DR   Bgee; ENSMUSG00000059456; Expressed in dentate gyrus of hippocampal formation granule cell and 184 other tissues.
DR   ExpressionAtlas; Q9QVP9; baseline and differential.
DR   Genevisible; Q9QVP9; MM.
DR   GO; GO:0097440; C:apical dendrite; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0044297; C:cell body; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0005938; C:cell cortex; ISO:MGI.
DR   GO; GO:0042995; C:cell projection; ISO:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0030425; C:dendrite; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0004972; F:NMDA glutamate receptor activity; ISO:MGI.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0043621; F:protein self-association; ISO:MGI.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR   GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR   GO; GO:0042976; P:activation of Janus kinase activity; ISO:MGI.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; ISO:MGI.
DR   GO; GO:0045453; P:bone resorption; IMP:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006968; P:cellular defense response; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IMP:MGI.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR   GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0060292; P:long-term synaptic depression; ISO:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR   GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IMP:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:MGI.
DR   GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR   GO; GO:0001556; P:oocyte maturation; ISO:MGI.
DR   GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:2000538; P:positive regulation of B cell chemotaxis; IMP:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR   GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:UniProtKB.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR   GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0010752; P:regulation of cGMP-mediated signaling; IMP:UniProtKB.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR   GO; GO:0032960; P:regulation of inositol trisphosphate biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0010758; P:regulation of macrophage chemotaxis; IMP:UniProtKB.
DR   GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:UniProtKB.
DR   GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR   GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0043157; P:response to cation stress; ISO:MGI.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; ISO:MGI.
DR   GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR   GO; GO:0043149; P:stress fiber assembly; ISO:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13190; FERM_C_FAK1; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR041390; FADK_N.
DR   InterPro; IPR041784; FAK1/PYK2_FERM_C.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR   InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR030610; PTK2B.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR24418:SF94; PTHR24418:SF94; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF18038; FERM_N_2; 1.
DR   Pfam; PF03623; Focal_AT; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF68993; SSF68993; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Angiogenesis; ATP-binding; Cell junction; Cell membrane;
KW   Cell projection; Cytoplasm; Direct protein sequencing; Immunity; Kinase;
KW   Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..1009
FT                   /note="Protein-tyrosine kinase 2-beta"
FT                   /id="PRO_0000088082"
FT   DOMAIN          39..359
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          425..683
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          696..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..1009
FT                   /note="Interaction with TGFB1I1"
FT                   /evidence="ECO:0000250"
FT   REGION          868..1009
FT                   /note="Focal adhesion targeting (FAT)"
FT   COMPBIAS        707..727
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        549
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         431..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         457
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         503..509
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         402
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11420674,
FT                   ECO:0000269|PubMed:11493697, ECO:0000269|PubMed:14739300,
FT                   ECO:0000269|PubMed:20688918, ECO:0000269|PubMed:21195757,
FT                   ECO:0007744|PubMed:17947660"
FT   MOD_RES         579
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:20688918,
FT                   ECO:0007744|PubMed:17947660"
FT   MOD_RES         580
FT                   /note="Phosphotyrosine; by SRC, FYN and LCK"
FT                   /evidence="ECO:0000269|PubMed:11420674,
FT                   ECO:0000269|PubMed:21195757, ECO:0007744|PubMed:17947660"
FT   MOD_RES         722
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         762
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         765
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         834
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         839
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         842
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         849
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         866
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14289"
FT   MOD_RES         881
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11420674,
FT                   ECO:0000269|PubMed:21195757"
FT   MUTAGEN         402
FT                   /note="Y->A: Loss of phosphorylation and interaction with
FT                   SRC, and inhibition of bone resorption."
FT                   /evidence="ECO:0000269|PubMed:14739300"
FT   CONFLICT        306
FT                   /note="K -> R (in Ref. 4; AAI37705/AAI44850)"
FT                   /evidence="ECO:0000305"
SQ   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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