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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_HUMAN              Reviewed;        1009 AA.
Q14289; D3DST0; Q13475; Q14290; Q16709; Q6PID4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
27-SEP-2017, entry version 201.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN REGULATION OF
POTASSIUM CHANNELS; PHOSPHORYLATION OF KCNA2 AND SHC1 AND ACTIVATION
OF MAPK1/ERK2, INTERACTION WITH GRB2, AND TISSUE SPECIFICITY.
TISSUE=Brain;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
PubMed=8838818; DOI=10.1006/geno.1996.0149;
Herzog H., Nicholl J., Hort Y.J., Sutherland G.R., Shine J.;
"Molecular cloning and assignment of FAK2, a novel human focal
adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization.";
Genomics 32:484-486(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION, AND TISSUE
SPECIFICITY.
TISSUE=Monocyte;
PubMed=9545257; DOI=10.1074/jbc.273.16.9361;
Li X., Hunter D., Morris J., Haskill J.S., Earp H.S.;
"A calcium-dependent tyrosine kinase splice variant in human
monocytes. Activation by a two-stage process involving adherence and a
subsequent intracellular signal.";
J. Biol. Chem. 273:9361-9364(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and Testis;
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).
[9]
FUNCTION IN PHOSPHORYLATION OF SRC AND ACTIVATION OF THE MAP KINASE
SIGNALING CASCADE, INTERACTION WITH SRC, AUTOPHOSPHORYLATION, AND
MUTAGENESIS OF TYR-402.
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).
[10]
FUNCTION IN TNF SIGNALING AND ACTIVATION OF MAPK8/JNK1.
PubMed=8670418; DOI=10.1126/science.273.5276.792;
Tokiwa G., Dikic I., Lev S., Schlessinger J.;
"Activation of Pyk2 by stress signals and coupling with JNK signaling
pathway.";
Science 273:792-794(1996).
[11]
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).
[12]
INTERACTION WITH ASAP2, AND FUNCTION.
PubMed=10022920; DOI=10.1128/MCB.19.3.2338;
Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G.,
Randazzo P.A., Schlessinger J.;
"Identification of a new Pyk2 target protein with Arf-GAP activity.";
Mol. Cell. Biol. 19:2338-2350(1999).
[13]
INTERACTION WITH RB1CC1.
PubMed=10769033; DOI=10.1083/jcb.149.2.423;
Ueda H., Abbi S., Zheng C., Guan J.-L.;
"Suppression of Pyk2 kinase and cellular activities by FIP200.";
J. Cell Biol. 149:423-430(2000).
[14]
PHOSPHORYLATION AT TYR-402, MUTAGENESIS OF PRO-859, 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).
[15]
FUNCTION IN ASAP1 PHOSPHORYLATION AND REGULATION OF ASAP1 ACTIVITY,
AND INTERACTION WITH ASAP1.
PubMed=12771146; DOI=10.1074/jbc.M302278200;
Kruljac-Letunic A., Moelleken J., Kallin A., Wieland F., Blaukat A.;
"The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation
and inhibition of the Arf-GTPase-activating protein ASAP1.";
J. Biol. Chem. 278:29560-29570(2003).
[16]
INTERACTION WITH SKAP2, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=12893833; DOI=10.1074/jbc.M213217200;
Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H.,
Avraham H., Avraham S., Yasuda M., Matsumoto M.;
"Identification and characterization of a novel Pyk2/related adhesion
focal tyrosine kinase-associated protein that inhibits alpha-synuclein
phosphorylation.";
J. Biol. Chem. 278:42225-42233(2003).
[17]
FUNCTION, INTERACTION WITH PDPK1, AND SUBCELLULAR LOCATION.
PubMed=14585963; DOI=10.1128/MCB.23.22.8019-8029.2003;
Taniyama Y., Weber D.S., Rocic P., Hilenski L., Akers M.L., Park J.,
Hemmings B.A., Alexander R.W., Griendling K.K.;
"Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates
focal adhesions.";
Mol. Cell. Biol. 23:8019-8029(2003).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[19]
FUNCTION IN INTEGRIN SIGNALING AND IN REGULATION OF CELL
PROLIFERATION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF ISOFORM 2.
PubMed=15050747; DOI=10.1016/j.exphem.2004.01.001;
Dylla S.J., Deyle D.R., Theunissen K., Padurean A.M., Verfaillie C.M.;
"Integrin engagement-induced inhibition of human myelopoiesis is
mediated by proline-rich tyrosine kinase 2 gene products.";
Exp. Hematol. 32:365-374(2004).
[20]
PHOSPHORYLATION AT TYR-402, CATALYTIC ACTIVITY, FUNCTION IN
SRC-MEDIATED PHOSPHORYLATION OF PXN, AND MUTAGENESIS OF LYS-457.
PubMed=15166227; DOI=10.1074/jbc.M313527200;
Park S.Y., Avraham H.K., Avraham S.;
"RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation
in a Src-independent manner.";
J. Biol. Chem. 279:33315-33322(2004).
[21]
INTERACTION WITH LPXN AND PTPN12, PHOSPHORYLATION AT TYR-402, AND
DEPHOSPHORYLATION BY PTPN12.
PubMed=17329398; DOI=10.1152/ajpcell.00503.2006;
Sahu S.N., Nunez S., Bai G., Gupta A.;
"Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer
cells.";
Am. J. Physiol. 292:C2288-C2296(2007).
[22]
FUNCTION IN MIGRATION OF T-LYMPHOCYTES, AND INTERACTION WITH EPHA1;
LCK AND PI3-KINASE.
PubMed=17634955; DOI=10.1002/eji.200737111;
Hjorthaug H.S., Aasheim H.C.;
"Ephrin-A1 stimulates migration of CD8+CCR7+ T lymphocytes.";
Eur. J. Immunol. 37:2326-2336(2007).
[23]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND ROLE IN DISEASE.
PubMed=18339875; DOI=10.1158/0008-5472.CAN-07-5155;
Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C.,
Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L.,
Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N.,
Schmitt E., LaGreca S., Jani J., Wessel M., Marr E., Griffor M.,
Vajdos F.;
"Antitumor activity and pharmacology of a selective focal adhesion
kinase inhibitor, PF-562,271.";
Cancer Res. 68:1935-1944(2008).
[24]
FUNCTION IN CELL ADHESION; MIGRATION; PROLIFERATION; REGULATION OF
ACTIN FIBER POLYMERIZATION AND IN ACTIVATION OF SRC; MAPK1/ERK2 AND
MAPK3/ERK1, INTERACTION WITH SRC, SUBCELLULAR LOCATION, AND ROLE IN
DISEASE.
PubMed=18765415; DOI=10.1093/carcin/bgn203;
Sun C.K., Man K., Ng K.T., Ho J.W., Lim Z.X., Cheng Q., Lo C.M.,
Poon R.T., Fan S.T.;
"Proline-rich tyrosine kinase 2 (Pyk2) promotes proliferation and
invasiveness of hepatocellular carcinoma cells through c-Src/ERK
activation.";
Carcinogenesis 29:2096-2105(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; THR-765; SER-839
AND THR-842, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[27]
INTERACTION WITH RHOU, AND FUNCTION IN REORGANIZATION OF ACTIN
CYTOSKELETON AND SRC-MEDIATED RHOU PHOSPHORYLATION.
PubMed=18086875; DOI=10.1128/MCB.00201-07;
Ruusala A., Aspenstrom P.;
"The atypical Rho GTPase Wrch1 collaborates with the nonreceptor
tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics.";
Mol. Cell. Biol. 28:1802-1814(2008).
[28]
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).
[29]
FUNCTION IN REGULATION OF ACTIN CYTOSKELETON REORGANIZATION AND
ACTIVATION OF RHO FAMILY GTPASES, PHOSPHORYLATION AT TYR-402,
SUBCELLULAR LOCATION, AND INTERACTION WITH VAV1.
PubMed=19207108; DOI=10.1042/BJ20090037;
Gao C., Blystone S.D.;
"A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate
Rho activation.";
Biochem. J. 420:49-56(2009).
[30]
ROLE IN DISEASE, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=19648005; DOI=10.1016/j.bmcl.2009.07.084;
Allen J.G., Lee M.R., Han C.Y., Scherrer J., Flynn S., Boucher C.,
Zhao H., O'Connor A.B., Roveto P., Bauer D., Graceffa R.,
Richards W.G., Babij P.;
"Identification of small molecule inhibitors of proline-rich tyrosine
kinase 2 (Pyk2) with osteogenic activity in osteoblast cells.";
Bioorg. Med. Chem. Lett. 19:4924-4928(2009).
[31]
FUNCTION IN CELL ADHESION AND SPREADING, AUTOPHOSPHORYLATION, AND
INTERACTION WITH BCAR1.
PubMed=19086031; DOI=10.1002/jcp.21649;
Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A.;
"Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and
regulates human glomerular mesangial cell adhesion and spreading.";
J. Cell. Physiol. 219:45-56(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-375; SER-399;
TYR-722; SER-762; TYR-819; TYR-834; SER-839; THR-842; TYR-849 AND
SER-866, VARIANT [LARGE SCALE ANALYSIS] THR-838, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[33]
FUNCTION IN IGF1 SIGNALING AND ACTIVATION OF MAPK1/ERK2 AND
MAPK3/ERK1, INTERACTION WITH SRC AND GRB2, PHOSPHORYLATION AT TYR-402
AND TYR-881, AND MUTAGENESIS OF TYR-881.
PubMed=20521079; DOI=10.1007/s00018-010-0411-x;
Shen X., Xi G., Radhakrishnan Y., Clemmons D.R.;
"Recruitment of Pyk2 to SHPS-1 signaling complex is required for IGF-
I-dependent mitogenic signaling in vascular smooth muscle cells.";
Cell. Mol. Life Sci. 67:3893-3903(2010).
[34]
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).
[35]
PHOSPHORYLATION AT TYR-402 AND TYR-580 BY FYN AND LCK.
PubMed=20028775; DOI=10.1189/jlb.0409227;
Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B.,
Houtman J.C.;
"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402
and 580 occurs via a distinct mechanism than other receptor systems.";
J. Leukoc. Biol. 87:691-701(2010).
[36]
FUNCTION IN T-CELL RECEPTOR-MEDIATED SIGNALING, AND PHOSPHORYLATION AT
TYR-402 AND TYR-580.
PubMed=20381867; DOI=10.1016/j.molimm.2010.03.009;
Collins M., Bartelt R.R., Houtman J.C.;
"T cell receptor activation leads to two distinct phases of Pyk2
activation and actin cytoskeletal rearrangement in human T cells.";
Mol. Immunol. 47:1665-1674(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
INTERACTION WITH NPHP1, AND FUNCTION IN PHOSPHORYLATION OF NPHP1.
PubMed=21357692; DOI=10.1074/jbc.M110.165464;
Liebau M.C., Hopker K., Muller R.U., Schmedding I., Zank S.,
Schairer B., Fabretti F., Hohne M., Bartram M.P., Dafinger C.,
Hackl M., Burst V., Habbig S., Zentgraf H., Blaukat A., Walz G.,
Benzing T., Schermer B.;
"Nephrocystin-4 regulates Pyk2-induced tyrosine phosphorylation of
nephrocystin-1 to control targeting to monocilia.";
J. Biol. Chem. 286:14237-14245(2011).
[39]
FUNCTION IN REORGANIZATION OF CYTOSKELETON; FORMATION OF MEMBRANE
RUFFLES AND CELL MIGRATION, AND ROLE IN DISEASE.
PubMed=21533080; DOI=10.1371/journal.pone.0018878;
Sun C.K., Ng K.T., Lim Z.X., Cheng Q., Lo C.M., Poon R.T., Man K.,
Wong N., Fan S.T.;
"Proline-rich tyrosine kinase 2 (Pyk2) promotes cell motility of
hepatocellular carcinoma through induction of epithelial to
mesenchymal transition.";
PLoS ONE 6:E18878-E18878(2011).
[40]
REVIEW ON ROLE IN IMMUNITY.
PubMed=15888917; DOI=10.1385/IR:31:3:267;
Ostergaard H.L., Lysechko T.L.;
"Focal adhesion kinase-related protein tyrosine kinase Pyk2 in T-cell
activation and function.";
Immunol. Res. 31:267-282(2005).
[41]
REVIEW ON FUNCTION; SIGNALING; INTERACTION PARTNERS; ENZYME
REGULATION; PHOSPHORYLATION, AND ROLE IN DISEASE.
PubMed=20001213; DOI=10.1517/14728220903473194;
Lipinski C.A., Loftus J.C.;
"Targeting Pyk2 for therapeutic intervention.";
Expert Opin. Ther. Targets 14:95-108(2010).
[42]
REVIEW.
PubMed=20332118; DOI=10.1242/jcs.045112;
Schaller M.D.;
"Cellular functions of FAK kinases: insight into molecular mechanisms
and novel functions.";
J. Cell Sci. 123:1007-1013(2010).
[43]
REVIEW ON ROLE IN DISEASE.
PubMed=21196189; DOI=10.2741/3706;
Felty Q.;
"Redox sensitive Pyk2 as a target for therapeutics in breast cancer.";
Front. Biosci. 16:568-577(2011).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND THR-842, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[45]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 416-692 IN COMPLEX WITH
PF-2318841, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=18951788; DOI=10.1016/j.bmcl.2008.10.030;
Walker D.P., Bi F.C., Kalgutkar A.S., Bauman J.N., Zhao S.X.,
Soglia J.R., Aspnes G.E., Kung D.W., Klug-McLeod J., Zawistoski M.P.,
McGlynn M.A., Oliver R., Dunn M., Li J.C., Richter D.T., Cooper B.A.,
Kath J.C., Hulford C.A., Autry C.L., Luzzio M.J., Ung E.J.,
Roberts W.G., Bonnette P.C., Buckbinder L., Mistry A., Griffor M.C.,
Han S., Guzman-Perez A.;
"Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine
kinase 2 (PYK2): structure-activity relationships and strategies for
the elimination of reactive metabolite formation.";
Bioorg. Med. Chem. Lett. 18:6071-6077(2008).
[46]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 861-1009 IN COMPLEX WITH PXN,
AND INTERACTION WITH PXN.
PubMed=19358827; DOI=10.1016/j.bbrc.2009.04.011;
Lulo J., Yuzawa S., Schlessinger J.;
"Crystal structures of free and ligand-bound focal adhesion targeting
domain of Pyk2.";
Biochem. Biophys. Res. Commun. 383:347-352(2009).
[47]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-692 IN COMPLEX WITH
INHIBITOR P1E, ROLE IN DISEASE, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=19428251; DOI=10.1016/j.bmcl.2009.04.093;
Walker D.P., Zawistoski M.P., McGlynn M.A., Li J.C., Kung D.W.,
Bonnette P.C., Baumann A., Buckbinder L., Houser J.A., Boer J.,
Mistry A., Han S., Xing L., Guzman-Perez A.;
"Sulfoximine-substituted trifluoromethylpyrimidine analogs as
inhibitors of proline-rich tyrosine kinase 2 (PYK2) show reduced hERG
activity.";
Bioorg. Med. Chem. Lett. 19:3253-3258(2009).
[48]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 416-692 IN COMPLEXES WITH
ATP ANALOG; PF-431396; BIRB796 AND PF-4618433, AND ROLE IN DISEASE.
PubMed=19244237; DOI=10.1074/jbc.M809038200;
Han S., Mistry A., Chang J.S., Cunningham D., Griffor M.,
Bonnette P.C., Wang H., Chrunyk B.A., Aspnes G.E., Walker D.P.,
Brosius A.D., Buckbinder L.;
"Structural characterization of proline-rich tyrosine kinase 2 (PYK2)
reveals a unique (DFG-out) conformation and enables inhibitor
design.";
J. Biol. Chem. 284:13193-13201(2009).
[49]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 414-692.
Structural genomics consortium (SGC);
"Structure of protein tyrosine kinase 2 beta (PTK2B) kinase domain.";
Submitted (JUL-2011) to the PDB data bank.
[50]
VARIANTS [LARGE SCALE ANALYSIS] GLU-359; HIS-698; PRO-808; THR-838 AND
LYS-970.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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'. 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. {ECO:0000269|PubMed:10022920,
ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:12893833,
ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:15050747,
ECO:0000269|PubMed:15166227, ECO:0000269|PubMed:17634955,
ECO:0000269|PubMed:18086875, ECO:0000269|PubMed:18339875,
ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18765415,
ECO:0000269|PubMed:19086031, ECO:0000269|PubMed:19207108,
ECO:0000269|PubMed:19244237, ECO:0000269|PubMed:19428251,
ECO:0000269|PubMed:19648005, ECO:0000269|PubMed:19880522,
ECO:0000269|PubMed:20001213, ECO:0000269|PubMed:20381867,
ECO:0000269|PubMed:20521079, ECO:0000269|PubMed:21357692,
ECO:0000269|PubMed:21533080, ECO:0000269|PubMed:7544443,
ECO:0000269|PubMed:8670418, ECO:0000269|PubMed:8849729}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:15050747,
ECO:0000269|PubMed:15166227, ECO:0000269|PubMed:18339875,
ECO:0000269|PubMed:18951788, ECO:0000269|PubMed:19428251,
ECO:0000269|PubMed:19648005}.
-!- 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. Inhibited by PF-562,271, BIRB796, PF-4618433 and by PF-
431396, PF-2318841 and their derivatives. Inhibited by
sulfoximine-substituted trifluoromethylpyrimidines. Inhibited by
4-amino and 5-aryl substituted pyridinone compounds.
{ECO:0000269|PubMed:18339875, ECO:0000269|PubMed:18951788,
ECO:0000269|PubMed:19428251, ECO:0000269|PubMed:19648005}.
-!- SUBUNIT: Homodimer, or homooligomer. Interacts with SIRPA and
SH2D3C. Interacts with ARHGAP10. Interacts with DLG4 (By
similarity). 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 PDPK1.
Interacts (hypophosphorylated) with PXN. Interacts with RB1CC1.
Interacts with RHOU. Interacts with VAV1. Interacts with LPXN and
PTPN12. {ECO:0000250|UniProtKB:P70600,
ECO:0000250|UniProtKB:Q9QVP9, ECO:0000269|PubMed:10022920,
ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:11493697,
ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:12893833,
ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:17329398,
ECO:0000269|PubMed:17634955, ECO:0000269|PubMed:18086875,
ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18765415,
ECO:0000269|PubMed:18951788, ECO:0000269|PubMed:19086031,
ECO:0000269|PubMed:19207108, ECO:0000269|PubMed:19358827,
ECO:0000269|PubMed:19428251, ECO:0000269|PubMed:20521079,
ECO:0000269|PubMed:21357692, ECO:0000269|PubMed:7544443,
ECO:0000269|PubMed:8849729, ECO:0000269|PubMed:9422762}.
-!- INTERACTION:
O75161:NPHP4; NbExp=2; IntAct=EBI-298640, EBI-4281852;
Q7L0Q8:RHOU; NbExp=4; IntAct=EBI-298640, EBI-1638043;
P12931:SRC; NbExp=3; IntAct=EBI-298640, EBI-621482;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell
junction, focal adhesion. Cell projection, lamellipodium.
Cytoplasm, cell cortex. Nucleus. Note=Interaction with NPHP1
induces the membrane-association of the kinase. Colocalizes with
integrins at the cell periphery.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14289-1; Sequence=Displayed;
Name=2; Synonyms=PYK2H;
IsoId=Q14289-2; Sequence=VSP_004981;
-!- TISSUE SPECIFICITY: Most abundant in the brain, with highest
levels in amygdala and hippocampus. Low levels in kidney (at
protein level). Also expressed in spleen and lymphocytes.
{ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:9545257}.
-!- 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.
{ECO:0000269|PubMed:11493697, ECO:0000269|PubMed:15166227,
ECO:0000269|PubMed:17329398, ECO:0000269|PubMed:18587400,
ECO:0000269|PubMed:19207108, ECO:0000269|PubMed:20028775,
ECO:0000269|PubMed:20381867, ECO:0000269|PubMed:20521079,
ECO:0000269|PubMed:9545257}.
-!- DISEASE: Note=Aberrant PTK2B/PYK2 expression may play a role in
cancer cell proliferation, migration and invasion, in tumor
formation and metastasis. Elevated PTK2B/PYK2 expression is seen
in gliomas, hepatocellular carcinoma, lung cancer and breast
cancer.
-!- MISCELLANEOUS: Promotes bone resorption, and thus PTK2B/PYK2
inhibitors might be used to treat osteoporosis.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; U33284; AAC50203.1; -; mRNA.
EMBL; L49207; AAB47217.1; -; mRNA.
EMBL; D45853; BAA08289.1; -; mRNA.
EMBL; U43522; AAC05330.1; -; mRNA.
EMBL; S80542; AAB35701.1; -; mRNA.
EMBL; AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63553.1; -; Genomic_DNA.
EMBL; CH471080; EAW63555.1; -; Genomic_DNA.
EMBL; CH471080; EAW63556.1; -; Genomic_DNA.
EMBL; BC036651; AAH36651.1; -; mRNA.
EMBL; BC042599; AAH42599.1; -; mRNA.
CCDS; CCDS6057.1; -. [Q14289-1]
CCDS; CCDS6058.1; -. [Q14289-2]
PIR; S60248; S60248.
RefSeq; NP_004094.3; NM_004103.4. [Q14289-1]
RefSeq; NP_775266.1; NM_173174.2. [Q14289-1]
RefSeq; NP_775267.1; NM_173175.2. [Q14289-2]
RefSeq; NP_775268.1; NM_173176.2. [Q14289-1]
RefSeq; XP_005273504.1; XM_005273447.4. [Q14289-1]
RefSeq; XP_011542743.1; XM_011544441.2. [Q14289-1]
RefSeq; XP_016868703.1; XM_017013214.1. [Q14289-1]
UniGene; Hs.491322; -.
UniGene; Hs.735450; -.
PDB; 2FO6; Model; -; X=45-350.
PDB; 2LK4; NMR; -; A=871-1005.
PDB; 3CC6; X-ray; 1.60 A; A=414-692.
PDB; 3ET7; X-ray; 2.70 A; A=416-692.
PDB; 3FZO; X-ray; 2.20 A; A=416-692.
PDB; 3FZP; X-ray; 2.10 A; A=416-692.
PDB; 3FZR; X-ray; 2.70 A; A=416-692.
PDB; 3FZS; X-ray; 1.75 A; A=416-692.
PDB; 3FZT; X-ray; 1.95 A; A=416-692.
PDB; 3GM1; X-ray; 2.95 A; A/B=861-1009.
PDB; 3GM2; X-ray; 2.71 A; A=861-1009.
PDB; 3GM3; X-ray; 2.60 A; A=861-1009.
PDB; 3H3C; X-ray; 2.00 A; A=416-692.
PDB; 3U3F; X-ray; 3.10 A; A/B/C/D=871-1005.
PDB; 4EKU; X-ray; 3.25 A; A=21-409.
PDB; 4H1J; X-ray; 2.00 A; A=416-692.
PDB; 4H1M; X-ray; 1.99 A; A=416-692.
PDB; 4R32; X-ray; 3.50 A; A=871-1005.
PDB; 4XEF; X-ray; 2.50 A; A/D=871-1005.
PDB; 4XEK; X-ray; 1.79 A; A=871-1005.
PDB; 4XEV; X-ray; 2.01 A; A/D=871-1005.
PDB; 5TO8; X-ray; 1.98 A; A=414-692.
PDBsum; 2FO6; -.
PDBsum; 2LK4; -.
PDBsum; 3CC6; -.
PDBsum; 3ET7; -.
PDBsum; 3FZO; -.
PDBsum; 3FZP; -.
PDBsum; 3FZR; -.
PDBsum; 3FZS; -.
PDBsum; 3FZT; -.
PDBsum; 3GM1; -.
PDBsum; 3GM2; -.
PDBsum; 3GM3; -.
PDBsum; 3H3C; -.
PDBsum; 3U3F; -.
PDBsum; 4EKU; -.
PDBsum; 4H1J; -.
PDBsum; 4H1M; -.
PDBsum; 4R32; -.
PDBsum; 4XEF; -.
PDBsum; 4XEK; -.
PDBsum; 4XEV; -.
PDBsum; 5TO8; -.
ProteinModelPortal; Q14289; -.
SMR; Q14289; -.
BioGrid; 108480; 63.
CORUM; Q14289; -.
ELM; Q14289; -.
IntAct; Q14289; 17.
MINT; MINT-1211326; -.
STRING; 9606.ENSP00000332816; -.
BindingDB; Q14289; -.
ChEMBL; CHEMBL5469; -.
DrugBank; DB01645; Genistein.
DrugBank; DB01097; Leflunomide.
GuidetoPHARMACOLOGY; 2181; -.
iPTMnet; Q14289; -.
PhosphoSitePlus; Q14289; -.
BioMuta; PTK2B; -.
DMDM; 3183003; -.
EPD; Q14289; -.
MaxQB; Q14289; -.
PaxDb; Q14289; -.
PeptideAtlas; Q14289; -.
PRIDE; Q14289; -.
TopDownProteomics; Q14289-2; -. [Q14289-2]
DNASU; 2185; -.
Ensembl; ENST00000346049; ENSP00000332816; ENSG00000120899. [Q14289-1]
Ensembl; ENST00000397501; ENSP00000380638; ENSG00000120899. [Q14289-1]
Ensembl; ENST00000420218; ENSP00000391995; ENSG00000120899. [Q14289-2]
Ensembl; ENST00000517339; ENSP00000427931; ENSG00000120899. [Q14289-2]
GeneID; 2185; -.
KEGG; hsa:2185; -.
UCSC; uc003xfn.3; human. [Q14289-1]
CTD; 2185; -.
DisGeNET; 2185; -.
EuPathDB; HostDB:ENSG00000120899.17; -.
GeneCards; PTK2B; -.
H-InvDB; HIX0168898; -.
HGNC; HGNC:9612; PTK2B.
HPA; CAB003850; -.
HPA; HPA026091; -.
HPA; HPA026276; -.
MIM; 601212; gene.
neXtProt; NX_Q14289; -.
OpenTargets; ENSG00000120899; -.
PharmGKB; PA33956; -.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000069938; -.
HOVERGEN; HBG004018; -.
InParanoid; Q14289; -.
KO; K05871; -.
OMA; QMLTASH; -.
OrthoDB; EOG091G03BN; -.
PhylomeDB; Q14289; -.
TreeFam; TF316643; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-391160; Signal regulatory protein family interactions.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-451927; Interleukin-2 family signaling.
SignaLink; Q14289; -.
SIGNOR; Q14289; -.
ChiTaRS; PTK2B; human.
EvolutionaryTrace; Q14289; -.
GeneWiki; PTK2B; -.
GenomeRNAi; 2185; -.
PRO; PR:Q14289; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000120899; -.
CleanEx; HS_PTK2B; -.
ExpressionAtlas; Q14289; baseline and differential.
Genevisible; Q14289; HS.
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:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030027; C:lamellipodium; IDA: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:UniProtKB.
GO; GO:0014069; C:postsynaptic density of dendrite; 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:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0004871; F:signal transducer activity; NAS:ProtInc.
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; IMP:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006968; P:cellular defense response; ISS: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; IMP:BHF-UCL.
GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS: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; IMP: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; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IMP:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP: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; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP: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; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP: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; IMP:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS: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; IEA:Ensembl.
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:0046777; P:protein autophosphorylation; TAS:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
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; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP: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; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000058; P:regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISS: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:0006950; P:response to stress; TAS:ProtInc.
GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
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; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
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:SF338; PTHR24418:SF338; 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;
3D-structure; Adaptive immunity; Alternative splicing; Angiogenesis;
ATP-binding; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Immunity; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transferase; Tyrosine-protein kinase.
CHAIN 1 1009 Protein-tyrosine kinase 2-beta.
/FTId=PRO_0000088081.
DOMAIN 39 359 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 425 683 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 431 439 ATP.
NP_BIND 503 509 ATP.
REGION 801 1009 Interaction with TGFB1I1. {ECO:0000250}.
REGION 868 1009 Focal adhesion targeting (FAT).
COMPBIAS 702 767 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.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 402 402 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11493697,
ECO:0000269|PubMed:15166227,
ECO:0000269|PubMed:17329398,
ECO:0000269|PubMed:19207108,
ECO:0000269|PubMed:20028775,
ECO:0000269|PubMed:20381867,
ECO:0000269|PubMed:20521079}.
MOD_RES 579 579 Phosphotyrosine; by SRC, LYN and LCK.
{ECO:0000250|UniProtKB:Q9QVP9}.
MOD_RES 580 580 Phosphotyrosine; by SRC, LYN and LCK.
{ECO:0000269|PubMed:20028775,
ECO:0000269|PubMed:20381867}.
MOD_RES 722 722 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 765 765 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 819 819 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 834 834 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 839 839 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 842 842 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 849 849 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 881 881 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:20521079}.
VAR_SEQ 739 780 Missing (in isoform 2).
{ECO:0000303|PubMed:9545257}.
/FTId=VSP_004981.
VARIANT 359 359 Q -> E (in dbSNP:rs56175011).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041687.
VARIANT 698 698 R -> H (in dbSNP:rs35174236).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041688.
VARIANT 808 808 L -> P (in dbSNP:rs55747955).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041689.
VARIANT 838 838 K -> T (in dbSNP:rs751019).
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_020284.
VARIANT 970 970 E -> K (in dbSNP:rs56263944).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041690.
MUTAGEN 402 402 Y->F: Abolishes autophosphorylation.
Abolishes interaction with SRC.
{ECO:0000269|PubMed:8849729}.
MUTAGEN 457 457 K->A: Abolishes kinase activity.
{ECO:0000269|PubMed:15166227}.
MUTAGEN 859 859 P->A: Loss of interaction with NPHP1.
{ECO:0000269|PubMed:11493697}.
MUTAGEN 881 881 Y->F: Loss of phosphorylation site.
Strongly reduced interaction with GRB2.
{ECO:0000269|PubMed:20521079}.
CONFLICT 23 23 A -> G (in Ref. 3; BAA08289/AAC05330).
{ECO:0000305}.
CONFLICT 256 256 G -> P (in Ref. 2; AAB47217).
{ECO:0000305}.
CONFLICT 435 435 F -> L (in Ref. 3; AAC05330).
{ECO:0000305}.
CONFLICT 780 780 R -> G (in Ref. 2; AAB47217).
{ECO:0000305}.
CONFLICT 985 985 V -> M (in Ref. 8; AAH36651).
{ECO:0000305}.
HELIX 35 37 {ECO:0000244|PDB:4EKU}.
STRAND 38 45 {ECO:0000244|PDB:4EKU}.
STRAND 48 50 {ECO:0000244|PDB:4EKU}.
HELIX 52 54 {ECO:0000244|PDB:4EKU}.
STRAND 55 62 {ECO:0000244|PDB:4EKU}.
HELIX 67 76 {ECO:0000244|PDB:4EKU}.
TURN 77 80 {ECO:0000244|PDB:4EKU}.
HELIX 87 89 {ECO:0000244|PDB:4EKU}.
STRAND 90 99 {ECO:0000244|PDB:4EKU}.
STRAND 102 105 {ECO:0000244|PDB:4EKU}.
HELIX 111 117 {ECO:0000244|PDB:4EKU}.
TURN 119 121 {ECO:0000244|PDB:4EKU}.
HELIX 124 126 {ECO:0000244|PDB:4EKU}.
STRAND 127 133 {ECO:0000244|PDB:4EKU}.
TURN 138 140 {ECO:0000244|PDB:4EKU}.
HELIX 141 144 {ECO:0000244|PDB:4EKU}.
HELIX 148 165 {ECO:0000244|PDB:4EKU}.
TURN 166 169 {ECO:0000244|PDB:4EKU}.
HELIX 172 186 {ECO:0000244|PDB:4EKU}.
TURN 187 189 {ECO:0000244|PDB:4EKU}.
HELIX 194 196 {ECO:0000244|PDB:4EKU}.
HELIX 198 207 {ECO:0000244|PDB:4EKU}.
HELIX 210 212 {ECO:0000244|PDB:4EKU}.
HELIX 216 221 {ECO:0000244|PDB:4EKU}.
HELIX 224 238 {ECO:0000244|PDB:4EKU}.
HELIX 243 254 {ECO:0000244|PDB:4EKU}.
STRAND 263 273 {ECO:0000244|PDB:4EKU}.
STRAND 277 282 {ECO:0000244|PDB:4EKU}.
STRAND 285 289 {ECO:0000244|PDB:4EKU}.
STRAND 297 300 {ECO:0000244|PDB:4EKU}.
HELIX 302 304 {ECO:0000244|PDB:4EKU}.
STRAND 310 313 {ECO:0000244|PDB:4EKU}.
TURN 314 316 {ECO:0000244|PDB:4EKU}.
STRAND 317 322 {ECO:0000244|PDB:4EKU}.
STRAND 331 336 {ECO:0000244|PDB:4EKU}.
HELIX 338 355 {ECO:0000244|PDB:4EKU}.
STRAND 356 360 {ECO:0000244|PDB:4EKU}.
HELIX 422 424 {ECO:0000244|PDB:3CC6}.
STRAND 425 433 {ECO:0000244|PDB:3CC6}.
STRAND 435 445 {ECO:0000244|PDB:3CC6}.
STRAND 447 449 {ECO:0000244|PDB:3FZR}.
STRAND 451 458 {ECO:0000244|PDB:3CC6}.
STRAND 461 463 {ECO:0000244|PDB:3FZO}.
HELIX 465 481 {ECO:0000244|PDB:3CC6}.
STRAND 489 493 {ECO:0000244|PDB:3CC6}.
STRAND 495 497 {ECO:0000244|PDB:3CC6}.
STRAND 499 503 {ECO:0000244|PDB:3CC6}.
HELIX 510 517 {ECO:0000244|PDB:3CC6}.
TURN 518 520 {ECO:0000244|PDB:3CC6}.
HELIX 523 542 {ECO:0000244|PDB:3CC6}.
STRAND 546 548 {ECO:0000244|PDB:5TO8}.
HELIX 552 554 {ECO:0000244|PDB:3CC6}.
STRAND 555 559 {ECO:0000244|PDB:3CC6}.
STRAND 562 565 {ECO:0000244|PDB:3CC6}.
HELIX 570 572 {ECO:0000244|PDB:3CC6}.
HELIX 589 591 {ECO:0000244|PDB:3CC6}.
HELIX 594 599 {ECO:0000244|PDB:3CC6}.
HELIX 604 619 {ECO:0000244|PDB:3CC6}.
TURN 620 622 {ECO:0000244|PDB:3CC6}.
TURN 625 628 {ECO:0000244|PDB:3CC6}.
HELIX 631 633 {ECO:0000244|PDB:3CC6}.
HELIX 634 640 {ECO:0000244|PDB:3CC6}.
HELIX 652 661 {ECO:0000244|PDB:3CC6}.
HELIX 666 668 {ECO:0000244|PDB:3CC6}.
HELIX 672 691 {ECO:0000244|PDB:3CC6}.
HELIX 879 897 {ECO:0000244|PDB:4XEK}.
HELIX 898 900 {ECO:0000244|PDB:3GM3}.
HELIX 903 905 {ECO:0000244|PDB:4XEK}.
HELIX 906 927 {ECO:0000244|PDB:4XEK}.
HELIX 928 930 {ECO:0000244|PDB:4XEK}.
HELIX 933 962 {ECO:0000244|PDB:4XEK}.
TURN 963 965 {ECO:0000244|PDB:4XEK}.
HELIX 969 1004 {ECO:0000244|PDB:4XEK}.
SEQUENCE 1009 AA; 115875 MW; 420B21046274E7C2 CRC64;
MSGVSEPLSR VKLGTLRRPE GPAEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK
CTVQTEIREI ITSILLSGRI GPNIRLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC
LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC
LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS
LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDAKPTCLA
EFKQIRSIRC LPLEEGQAVL QLGIEGAPQA LSIKTSSLAE AENMADLIDG YCRLQGEHQG
SLIIHPRKDG EKRNSLPQIP MLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGI
AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN
LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVLTLVLYS LQICKAMAYL
ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPDLC PPVLYTLMTR
CWDYDPSDRP RFTELVCSLS DVYQMEKDIA MEQERNARYR TPKILEPTAF QEPPPKPSRP
KYRPPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR
EEDFIQPSSR EEAQQLWEAE KVKMRQILDK QQKQMVEDYQ WLRQEEKSLD PMVYMNDKSP
LTPEKEVGYL EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YLNVMELVRA VLELKNELCQ
LPPEGYVVVV KNVGLTLRKL IGSVDDLLPS LPSSSRTEIE GTQKLLNKDL AELINKMRLA
QQNAVTSLSE ECKRQMLTAS HTLAVDAKNL LDAVDQAKVL ANLAHPPAE


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