Protein-tyrosine kinase 2-beta - Mus musculus (Mouse)

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Q9QVP9 (FAK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein-tyrosine kinase 2-beta
EC=2.7.10.2

Alternative name(s):
Calcium-dependent tyrosine kinase
Short name=CADTK
Calcium-regulated non-receptor proline-rich tyrosine kinase
Cell adhesion kinase beta
Short name=CAK-beta
Short name=CAKB
Focal adhesion kinase 2
Short name=FADK 2
Proline-rich tyrosine kinase 2
Related adhesion focal tyrosine kinase
Short name=RAFTK

Gene names

Name:	Ptk2b
Synonyms:	Fak2, Pyk2, Raftk

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1009 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T cells, and contributes to the regulation of T cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' By similarity. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca²⁺ levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 By similarity. Ref.7 Ref.8 Ref.12 Ref.13 Ref.16 Ref.17 Ref.19 Ref.22 Ref.24 Ref.25 Ref.26 Ref.28
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.19
Enzyme regulation	Activated in response to stimuli that lead to increased intracellular Ca²⁺ 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. Ref.19 Ref.26
Subunit structure	Homodimer, or homooligomer. Interacts with NPHP1, ASAP1, ASAP2, ARHGAP26, SKAP2 and TGFB1I1. The Tyr-402 phosphorylated form interacts with SRC (via SH2 domain) and SRC family members. Forms a signaling complex with EPHA1, LCK and phosphatidylinositol 3-kinase; upon activation by EFNA1. Interacts with GRB2 (via SH2 domain). Interacts with P53/TP53 and MDM2. Interacts with MYLK. Interacts with BCAR1. Interacts with RB1CC1. Interacts with RHOU. Interacts with VAV1. Interacts with PDPK1. Interacts with DLG4. Interacts with LPXN and PTPN12 By similarity. Interacts with SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts with ARHGAP10. Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.13 Ref.16 Ref.22 Ref.27
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › focal adhesion. Cell projection › lamellipodium By similarity. Cytoplasm › cell cortex By similarity. Nucleus By similarity. Note: Colocalizes with integrins at the cell periphery By similarity. Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts. Ref.25 Ref.27
Post-translational modification	Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration; this activation is indirect and may be mediated by production of reactive oxygen species (ROS). Tyr-402 is the major autophosphorylation site, but other kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-402 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is important for interaction with GRB2. Phosphorylated on tyrosine residues upon activation of FGR and PKC. Recruitment by NPHP1 to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity. Phosphorylation by MYLK promotes ITGB2 activation and is thus essential to trigger neutrophil transmigration during lung injury. Dephosphorylated by PTPN12 By similarity. Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.27
Disruption phenotype	Mice are born at the expected Mendelian rate, appear normal and are fertile. Mice display increased bone formation and high bone mass, due to defects in osteoclastic bone resorption. Osteoclasts display defects in actin cytoskeleton reorganization, plus altered Rho activity, microtubule stabilization and podosome organization. Mice also display increased differentiation and activity of osteoprogenitor cells. Macrophages from mutant mice display defects in their responses to chemokines, including defects in cell polarization, actin cytoskeleton reorganization, directed migration towards sites of inflammation, but also defects in the regulation of intracellular Ca²⁺ levels, phosphatidylinositol 3-kinase activity and inositol-1,4,5-trisphosphate production. Mutant mice have normal B cell polpulations in bone marrow, lymph nodes and blood, but lack marginal zone B-cells in the spleen. Ref.7 Ref.12 Ref.17 Ref.19
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Adaptive immunity Angiogenesis Immunity
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	bone resorption Inferred from mutant phenotype Ref.13. Source: UniProtKB signal complex assembly Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: InterPro focal adhesion Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction Ref.13. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1009

1009

Protein-tyrosine kinase 2-beta

PRO_0000088082

Regions

Domain

39 – 359

321

FERM

Domain

425 – 683

259

Protein kinase

Nucleotide binding

431 – 439

ATP By similarity

Nucleotide binding

503 – 509

ATP By similarity

Region

801 – 1009

209

Interaction with TGFB1I1 By similarity

Region

868 – 1009

142

Focal adhesion targeting (FAT)

Compositional bias

701 – 767

Pro-rich

Compositional bias

831 – 869

Pro-rich

Sites

Active site

549

Proton acceptor By similarity

Binding site

457

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

361

Phosphoserine By similarity

Modified residue

375

Phosphoserine Ref.15 Ref.21 Ref.23

Modified residue

389

Phosphoserine By similarity

Modified residue

392

Phosphoserine By similarity

Modified residue

394

Phosphoserine By similarity

Modified residue

396

Phosphoserine By similarity

Modified residue

399

Phosphoserine By similarity

Modified residue

402

Phosphotyrosine; by autocatalysis Ref.9 Ref.10 Ref.13 Ref.18 Ref.27

Modified residue

440

Phosphotyrosine Ref.20

Modified residue

559

Phosphoserine By similarity

Modified residue

579

Phosphotyrosine; by SRC, LYN and LCK Ref.18

Modified residue

580

Phosphotyrosine; by SRC, LYN and LCK Ref.9 Ref.18 Ref.27

Modified residue

583

Phosphoserine By similarity

Modified residue

722

Phosphotyrosine By similarity

Modified residue

746

Phosphoserine By similarity

Modified residue

758

Phosphoserine By similarity

Modified residue

762

Phosphoserine By similarity

Modified residue

765

Phosphothreonine By similarity

Modified residue

778

Phosphoserine By similarity

Modified residue

834

Phosphotyrosine By similarity

Modified residue

839

Phosphoserine By similarity

Modified residue

842

Phosphothreonine By similarity

Modified residue

849

Phosphotyrosine By similarity

Modified residue

866

Phosphoserine By similarity

Modified residue

881

Phosphotyrosine Ref.9 Ref.27

Modified residue

966

Phosphothreonine By similarity

Experimental info

Mutagenesis

402

Y → A: Loss of phosphorylation and interaction with SRC, and inhibition of bone resorption. Ref.13

Sequences

Sequence

Length

Mass (Da)

Tools

Q9QVP9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 963959FF56DF9605
Show »

FASTA

1,009

115,822

        10         20         30         40         50         60 
MSGVSEPLSR VKVGTLRRPE GPPEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK 

        70         80         90        100        110        120 
CTVQTEIQEI ITSILLSGRI GPNIQLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC 

       130        140        150        160        170        180 
LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC 

       190        200        210        220        230        240 
LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS 

       250        260        270        280        290        300 
LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDTKPTCLA 

       310        320        330        340        350        360 
EFKQIRSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG YCRLQGEHKG 

       370        380        390        400        410        420 
SLIMHAKKDG EKRNSLPQIP TLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGV 

       430        440        450        460        470        480 
AREEVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTQDNKEK FMSEAVIMKN 

       490        500        510        520        530        540 
LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVPTLVLYT LQICKAMAYL 

       550        560        570        580        590        600 
ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR 

       610        620        630        640        650        660 
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPELC PPVLYTLMTR 

       670        680        690        700        710        720 
CWDYDPSDRP RFTELVCSLS DIYQMEKDIA IEQERNARYR PPKILEPTTF QEPPPKPSRP 

       730        740        750        760        770        780 
KYRPPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR 

       790        800        810        820        830        840 
EEDFIRPSSR EEAQQLWEAE KIKMKQVLER QQKQMVEDSQ WLRREERCLD PMVYMNDKSP 

       850        860        870        880        890        900 
LTPEKEAGYT EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLGQ 

       910        920        930        940        950        960 
LPPEDYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL AELINKMKLA 

       970        980        990       1000 
QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV ANLAHPPAE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain." 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. J. Biol. Chem. 270:27742-27751(1995) [PubMed: 7499242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 469-479, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[4]	"The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells." Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A., Sattler M., Avraham H., Griffin J.D. J. Biol. Chem. 271:31222-31226(1996) [PubMed: 8940124] [Abstract] Cited for: INTERACTION WITH PXN.
[5]	"Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions." Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T. J. Biol. Chem. 273:1003-1014(1998) [PubMed: 9422762] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[6]	"SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages." Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E., Schraven B., Neel B.G. Curr. Biol. 9:927-930(1999) [PubMed: 10469599] [Abstract] Cited for: INTERACTION WITH SIRPA.
[7]	"Absence of marginal zone B cells in Pyk-2-deficient mice defines their role in the humoral response." Guinamard R., Okigaki M., Schlessinger J., Ravetch J.V. Nat. Immunol. 1:31-36(2000) [PubMed: 10881171] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B-CELL DIFFERENTIATION; B-CELL CHEMOTAXIS AND IMMUNE RESPONSE.
[8]	"Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting with PSGAP, a novel pleckstrin homology and Src homology 3 domain containing rhoGAP protein." Ren X.-R., Du Q.-S., Huang Y.-Z., Ao S.-Z., Mei L., Xiong W.-C. J. Cell Biol. 152:971-984(2001) [PubMed: 11238453] [Abstract] Cited for: INTERACTION WITH ARHGAP10, FUNCTION IN REGULATION OF ARHGAP10 ACTIVITY AND ACTIVATION OF CDC42 AND RHOA.
[9]	"Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration: analysis of specific phosphorylation events using site-directed antibodies." Nakamura K., Yano H., Schaefer E., Sabe H. Oncogene 20:2626-2635(2001) [PubMed: 11420674] [Abstract] Cited for: PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
[10]	"Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2." Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G. Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001) [PubMed: 11493697] [Abstract] Cited for: PHOSPHORYLATION AT TYR-402, INTERACTION WITH NPHP1.
[11]	"A novel hematopoietic adaptor protein, Chat-H, positively regulates T cell receptor-mediated interleukin-2 production by Jurkat cells." Sakakibara A., Hattori S., Nakamura S., Katagiri T. J. Biol. Chem. 278:6012-6017(2003) [PubMed: 12486027] [Abstract] Cited for: INTERACTION WITH SH2D3C.
[12]	"Pyk2 regulates multiple signaling events crucial for macrophage morphology and migration." Okigaki M., Davis C., Falasca M., Harroch S., Felsenfeld D.P., Sheetz M.P., Schlessinger J. Proc. Natl. Acad. Sci. U.S.A. 100:10740-10745(2003) [PubMed: 12960403] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[13]	"Src kinase activity is essential for osteoclast function." Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R. J. Biol. Chem. 279:17660-17666(2004) [PubMed: 14739300] [Abstract] Cited for: FUNCTION IN BONE RESORPTION, INTERACTION WITH SRC, PHOSPHORYLATION AT TYR-402, MUTAGENESIS OF TYR-402.
[14]	"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization." Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G. Exp. Cell Res. 302:253-269(2005) [PubMed: 15561106] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FGR.
[15]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY. Tissue: Brain.
[16]	"Central role of calcium-dependent tyrosine kinase PYK2 in endothelial nitric oxide synthase-mediated angiogenic response and vascular function." Matsui A., Okigaki M., Amano K., Adachi Y., Jin D., Takai S., Yamashita T., Kawashima S., Kurihara T., Miyazaki M., Tateishi K., Matsunaga S., Katsume A., Honshou S., Takahashi T., Matoba S., Kusaba T., Tatsumi T., Matsubara H. Circulation 116:1041-1051(2007) [PubMed: 17698736] [Abstract] Cited for: FUNCTION IN VEGFA SIGNALING; REGULATION OF INTRACELLULAR CALCIUM LEVELS; ACTIVATION OF AKT1 AND RAC1; PHOSPHORYLATION OF SRC; REORGANIZATION OF ACTIN CYTOSKELETON; CELL MIGRATION AND ANGIOGENESIS, INTERACTION WITH SRC.
[17]	"Defective microtubule-dependent podosome organization in osteoclasts leads to increased bone density in Pyk2(-/-) mice." Gil-Henn H., Destaing O., Sims N.A., Aoki K., Alles N., Neff L., Sanjay A., Bruzzaniti A., De Camilli P., Baron R., Schlessinger J. J. Cell Biol. 178:1053-1064(2007) [PubMed: 17846174] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[18]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; TYR-579 AND TYR-580, MASS SPECTROMETRY. Tissue: Mast cell.
[19]	"Proline-rich tyrosine kinase 2 regulates osteoprogenitor cells and bone formation, and offers an anabolic treatment approach for osteoporosis." Buckbinder L., Crawford D.T., Qi H., Ke H.Z., Olson L.M., Long K.R., Bonnette P.C., Baumann A.P., Hambor J.E., Grasser W.A. III, Pan L.C., Owen T.A., Luzzio M.J., Hulford C.A., Gebhard D.F., Paralkar V.M., Simmons H.A., Kath J.C. Li M. Proc. Natl. Acad. Sci. U.S.A. 104:10619-10624(2007) [PubMed: 17537919] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
[20]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-440, MASS SPECTROMETRY. Tissue: Brain.
[21]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY. Tissue: Melanoma.
[22]	"Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins." Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B. Nat. Immunol. 9:880-886(2008) [PubMed: 18587400] [Abstract] Cited for: FUNCTION DURING LUNG INJURY, PHOSPHORYLATION BY MYLK, INTERACTION WITH MYLK.
[23]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY. Tissue: Macrophage.
[24]	"B cell receptor-induced phosphorylation of Pyk2 and focal adhesion kinase involves integrins and the Rap GTPases and is required for B cell spreading." Tse K.W., Dang-Lawson M., Lee R.L., Vong D., Bulic A., Buckbinder L., Gold M.R. J. Biol. Chem. 284:22865-22877(2009) [PubMed: 19561089] [Abstract] Cited for: FUNCTION.
[25]	"Pyk2 inhibition of p53 as an adaptive and intrinsic mechanism facilitating cell proliferation and survival." Lim S.T., Miller N.L., Nam J.O., Chen X.L., Lim Y., Schlaepfer D.D. J. Biol. Chem. 285:1743-1753(2010) [PubMed: 19880522] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION AND REGULATION OT P53/TP53 UBIQUITINATION, SUBCELLULAR LOCATION.
[26]	"Regulation of the tyrosine kinase Pyk2 by calcium is through production of reactive oxygen species in cytotoxic T lymphocytes." Lysechko T.L., Cheung S.M., Ostergaard H.L. J. Biol. Chem. 285:31174-31184(2010) [PubMed: 20688918] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, ENZYME REGULATION.
[27]	"Hypophosphorylated and inactive Pyk2 associates with paxillin at the microtubule organizing center in hematopoietic cells." St-Pierre J., Lysechko T.L., Ostergaard H.L. Cell. Signal. 23:718-730(2011) [PubMed: 21195757] [Abstract] Cited for: INTERACTION WITH PXN, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
[28]	"Decreased cell adhesion promotes angiogenesis in a Pyk2-dependent manner." Shen C.J., Raghavan S., Xu Z., Baranski J.D., Yu X., Wozniak M.A., Miller J.S., Gupta M., Buckbinder L., Chen C.S. Exp. Cell Res. 317:1860-1871(2011) [PubMed: 21640103] [Abstract] Cited for: FUNCTION IN SPROUTING ANGIOGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC137704 mRNA. Translation: AAI37705.1. BC144849 mRNA. Translation: AAI44850.1.
IPI	IPI00133132.
UniGene	Mm.21613.
3D structure databases
ProteinModelPortal	Q9QVP9.
SMR	Q9QVP9. Positions 39-692, 867-1007.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QVP9. 3 interactions.
MINT	MINT-266339.
STRING	Q9QVP9.
PTM databases
PhosphoSite	Q9QVP9.
Proteomic databases
PRIDE	Q9QVP9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc011znr.1. mouse.
Organism-specific databases
MGI	MGI:104908. Ptk2b.
Phylogenomic databases
GeneTree	ENSGT00600000084269.
HOGENOM	HBG444482.
HOVERGEN	HBG004018.
InParanoid	Q9QVP9.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Gene expression databases
ArrayExpress	Q9QVP9.
Bgee	Q9QVP9.
CleanEx	MM_PTK2B.
Genevestigator	Q9QVP9.
GermOnline	ENSMUSG00000059456. Mus musculus.
Family and domain databases
InterPro	IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR000299. FERM_domain. IPR005189. Focal_adhesion_kin_target_dom. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Gene3D	G3DSA:1.20.80.10. ACBP. 1 hit.
Pfam	PF00373. FERM_M. 1 hit. PF03623. Focal_AT. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD006413. Focal_adhesion_target_reg. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00295. B41. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit. SSF68993. Focal_AT. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS00660. FERM_1. False negative. PS00661. FERM_2. False negative. PS50057. FERM_3. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
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Entry information

Entry name

FAK2_MOUSE

Accession

Primary (citable) accession number: Q9QVP9
Secondary accession number(s): B2RQ16

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents