P70600 (FAK2_RAT) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:	Ptk2b
Synonyms:	Fak2, Pyk2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.10
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 By similarity.
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 LPXN and PTPN12 By similarity. Interacts with SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts with ARHGAP10. Ref.6 Ref.7 Ref.11 Ref.13
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › lamellipodium By similarity. Cytoplasm › cell cortex By similarity. Nucleus By similarity. Note: Colocalizes with integrins at the cell periphery. Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts By similarity. Ref.3 Isoform 2: Cell junction › focal adhesion. Note: Localizes to focal adhesions, but not isoform 1 and isoform 3. Ref.3
Tissue specificity	Highly expressed in pulmonary vein endothelial cells, lung and brain (at protein level). Isoform 1 is expressed at high levels in the brain (hippocampus, cerebral cortex and olfactory bulb) and poorly in the spleen and other tissues, whereas isoforms 2 and 3 are expressed in the spleen and brain (highest in cerebellum). Ref.8
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.5 Ref.6 Ref.10 Ref.11 Ref.13
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
Coding sequence diversity	Alternative splicing
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	MAPK cascade Inferred from mutant phenotype PubMed 15096502. Source: RGD activation of Janus kinase activity Inferred from mutant phenotype PubMed 11818507. Source: RGD activation of Rac GTPase activity Inferred from mutant phenotype PubMed 15158121. Source: RGD blood vessel endothelial cell migration Inferred from mutant phenotype Ref.8. Source: RGD bone resorption Inferred from sequence or structural similarity. Source: UniProtKB cellular response to retinoic acid Inferred from electronic annotation. Source: Compara chemokine-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB elevation of cytosolic calcium ion concentration Inferred from mutant phenotype PubMed 11739373. Source: RGD epidermal growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 16945503. Source: RGD focal adhesion assembly Inferred from mutant phenotype PubMed 14585963. Source: RGD glial cell proliferation Inferred from expression pattern PubMed 11389173. Source: RGD integrin-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB marginal zone B cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of bone mineralization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of muscle cell apoptotic process Inferred from mutant phenotype PubMed 12668584. Source: RGD negative regulation of myeloid cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of potassium ion transport Inferred from electronic annotation. Source: Compara neuron projection development Inferred from mutant phenotype PubMed 10980697. Source: RGD oocyte maturation Inferred from mutant phenotype PubMed 17127746. Source: RGD positive regulation of B cell chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of JNK cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of JUN kinase activity Inferred from mutant phenotype PubMed 15226266. Source: RGD positive regulation of actin filament polymerization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from mutant phenotype PubMed 15158121. Source: RGD positive regulation of cell proliferation Inferred from expression pattern PubMed 11352836. Source: RGD positive regulation of cell-matrix adhesion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of endothelial cell migration Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase activity Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 15158121. Source: RGD positive regulation of translation Inferred from mutant phenotype PubMed 12890645. Source: RGD regulation of actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB regulation of cGMP biosynthetic process Inferred from electronic annotation. Source: Compara regulation of cGMP-mediated signaling Inferred from electronic annotation. Source: Compara regulation of calcium-mediated signaling Inferred from electronic annotation. Source: Compara regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of establishment of cell polarity Inferred from sequence or structural similarity. Source: UniProtKB regulation of inositol trisphosphate biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of macrophage chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara regulation of release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB response to cAMP Inferred from expression pattern PubMed 16120467. Source: RGD response to calcium ion Inferred from expression pattern PubMed 16120467PubMed 16945503. Source: RGD response to cocaine Inferred from expression pattern PubMed 12117546. Source: RGD response to drug Inferred from expression pattern PubMed 11139427. Source: RGD response to ethanol Inferred from expression pattern PubMed 12684223. Source: RGD response to glucose stimulus Inferred from expression pattern PubMed 11463795. Source: RGD response to hormone stimulus Inferred from expression pattern PubMed 16713446. Source: RGD response to hydrogen peroxide Inferred from physical interaction PubMed 16187300. Source: RGD response to hypoxia Inferred from expression pattern PubMed 11781137. Source: RGD response to lithium ion Inferred from expression pattern PubMed 15236860. Source: RGD response to mechanical stimulus Inferred from expression pattern PubMed 15096502. Source: RGD response to osmotic stress Inferred from expression pattern PubMed 11530010. Source: RGD signal complex assembly Inferred from electronic annotation. Source: InterPro sprouting angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB stress fiber assembly Inferred from mutant phenotype Ref.8. Source: RGD tumor necrosis factor-mediated signaling pathway Inferred from electronic annotation. Source: Compara vascular endothelial growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from direct assay PubMed 15128873. Source: RGD cell cortex Inferred from direct assay PubMed 17127746. Source: RGD focal adhesion Inferred from direct assay PubMed 17157995. Source: RGD growth cone Inferred from direct assay PubMed 15128873. Source: RGD lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB membrane raft Inferred from direct assay PubMed 15128873. Source: RGD nucleus Inferred from direct assay PubMed 16945503. Source: RGD perinuclear region of cytoplasm Inferred from direct assay PubMed 16945503. Source: RGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from direct assay PubMed 16600505. Source: RGD
Molecular_function	3-phosphoinositide-dependent protein kinase binding Inferred from direct assay PubMed 14585963. Source: RGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70600-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P70600-2)

Also known as: PRNK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-771: Missing.
     772-780: NVFKRHSMR → MGLIVLSSQ

Isoform 3 (identifier: P70600-3)

Also known as: PYK2s;

The sequence of this isoform differs from the canonical sequence as follows:
     739-780: Missing.

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_0000088083
Regions
	Domain	39 – 359	321	FERM
	Domain	425 – 683	259	Protein kinase
	Nucleotide binding	431 – 439	9	ATP By similarity
	Nucleotide binding	503 – 509	7	ATP By similarity
	Region	801 – 1009	209	Interaction with TGFB1I1
	Region	868 – 1009	142	Focal adhesion targeting (FAT)
	Compositional bias	701 – 767	67	Pro-rich
	Compositional bias	831 – 869	39	Pro-rich
Sites
	Active site	549	1	Proton acceptor By similarity
	Binding site	457	1	ATP By similarity
Amino acid modifications
	Modified residue	361	1	Phosphoserine By similarity
	Modified residue	375	1	Phosphoserine By similarity
	Modified residue	399	1	Phosphoserine By similarity
	Modified residue	402	1	Phosphotyrosine; by autocatalysis Ref.10 Ref.13
	Modified residue	440	1	Phosphotyrosine By similarity
	Modified residue	579	1	Phosphotyrosine; by SRC, LYN and LCK Ref.13
	Modified residue	580	1	Phosphotyrosine; by SRC, LYN and LCK Ref.10 Ref.13
	Modified residue	722	1	Phosphotyrosine By similarity
	Modified residue	762	1	Phosphoserine By similarity
	Modified residue	765	1	Phosphothreonine By similarity
	Modified residue	834	1	Phosphotyrosine By similarity
	Modified residue	839	1	Phosphoserine By similarity
	Modified residue	842	1	Phosphothreonine By similarity
	Modified residue	849	1	Phosphotyrosine By similarity
	Modified residue	866	1	Phosphoserine By similarity
	Modified residue	881	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	1 – 771	771	Missing in isoform 2.		VSP_004982
	Alternative sequence	739 – 780	42	Missing in isoform 3.		VSP_004984
	Alternative sequence	772 – 780	9	NVFKRHSMR → MGLIVLSSQ in isoform 2.		VSP_004983
Experimental info
	Sequence conflict	205	1	E → A in BAA08290. Ref.2
	Sequence conflict	807	1	V → F in AAC28340. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: D435A475BCA49E9B	FASTA	1,009	115,784
	10 20 30 40 50 60 MSGVSEPLSR VKVGTLRPPE 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 SLIIHAKKDG EKRNSLPQIP TLNLESRRSH LSESCSIESD IYAEIPDETL RRPGGPQYGV 430 440 450 460 470 480 AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN 490 500 510 520 530 540 LDHPHIVKLI GIIEEEPTWI VMELYPYGEL GHYLERNKNS LKVPTLVLYA 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 DIYQMERDIA IEQERNARYR PPKILEPTAF QEPPPKPSRP 730 740 750 760 770 780 KYKHPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR 790 800 810 820 830 840 EEDFIRPSSR EEAQQLWEAE KIKMRQVLDR QQKQMVEDSQ WLRREERCLD PMVYMNDKSP 850 860 870 880 890 900 LTPEKEAGYT EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLSQ 910 920 930 940 950 960 LPPEEYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL AELINKMRLA 970 980 990 1000 QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV ANLAHPPAE
	Isoform 2 (PRNK) [UniParc]. Checksum: 223D384D7CE2F9F4	FASTA	238	26,808
	10 20 30 40 50 60 MGLIVLSSQE EDFIRPSSRE EAQQLWEAEK IKMRQVLDRQ QKQMVEDSQW LRREERCLDP 70 80 90 100 110 120 MVYMNDKSPL TPEKEAGYTE FTGPPQKPPR LGAQSIQPTA NLDRTDDLVY HNVMTLVEAV 130 140 150 160 170 180 LELKNKLSQL PPEEYVVVVK NVGLNLRKLI GSVDDLLPSL PASSRTEIEG TQKLLNKDLA 190 200 210 220 230 ELINKMRLAQ QNAVTSLSED CKRQMLTASH TLAVDAKNLL DAVDQAKVVA NLAHPPAE
	Isoform 3 (PYK2s) [UniParc]. Checksum: CE6F8A2223E69167	FASTA	967	111,093
	10 20 30 40 50 60 MSGVSEPLSR VKVGTLRPPE 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 SLIIHAKKDG EKRNSLPQIP TLNLESRRSH LSESCSIESD IYAEIPDETL RRPGGPQYGV 430 440 450 460 470 480 AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN 490 500 510 520 530 540 LDHPHIVKLI GIIEEEPTWI VMELYPYGEL GHYLERNKNS LKVPTLVLYA 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 DIYQMERDIA IEQERNARYR PPKILEPTAF QEPPPKPSRP 730 740 750 760 770 780 KYKHPPQTNL LAPKLQFQEE DFIRPSSREE AQQLWEAEKI KMRQVLDRQQ KQMVEDSQWL 790 800 810 820 830 840 RREERCLDPM VYMNDKSPLT PEKEAGYTEF TGPPQKPPRL GAQSIQPTAN LDRTDDLVYH 850 860 870 880 890 900 NVMTLVEAVL ELKNKLSQLP PEEYVVVVKN VGLNLRKLIG SVDDLLPSLP ASSRTEIEGT 910 920 930 940 950 960 QKLLNKDLAE LINKMRLAQQ NAVTSLSEDC KRQMLTASHT LAVDAKNLLD AVDQAKVVAN LAHPPAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation." Yu H., Li X., Marchetto G.S., Dy R., Hunter D., Calvo B., Dawson T.L., Wilm M., Anderegg R.J., Graves L.M., Earp H.S. J. Biol. Chem. 271:29993-29998(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 310-334; 553-572; 672-687 AND 989-998. Tissue: Liver epithelium.
[2]	"Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily." Sasaki H., Nagura K., Ishino M., Tobioka H., Kotani K., Sasaki T. J. Biol. Chem. 270:21206-21219(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Sprague-Dawley. Tissue: Brain.
[3]	"Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein." Xiong W.-C., Macklem M., Parsons J.T. J. Cell Sci. 111:1981-1991(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, DOMAIN FAT. Tissue: Hippocampus.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Prostate.
[5]	"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions." Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J. Nature 376:737-745(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[6]	"A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation." Dikic I., Tokiwa G., Lev S., Courtneidge S.A., Schlessinger J. Nature 383:547-550(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN G-PROTEIN COUPLED RECEPTOR SIGNALING AND PHOSPHORYLATION OF SRC, INTERACTION WITH SRC, PHOSPHORYLATION.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[8]	"Pyk2/CAKbeta tyrosine kinase activity-mediated angiogenesis of pulmonary vascular endothelial cells." Tang H., Hao Q., Fitzgerald T., Sasaki T., Landon E.J., Inagami T. J. Biol. Chem. 277:5441-5447(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ANGIOGENESIS; CELL MIGRATION; CELL SPREADING AND REORGANIZATION OF THE ACTIN CYTOSKELETON, TISSUE SPECIFICITY.
[9]	"Metabotropic glutamate receptor 1-induced upregulation of NMDA receptor current: mediation through the Pyk2/Src-family kinase pathway in cortical neurons." Heidinger V., Manzerra P., Wang X.Q., Strasser U., Yu S.P., Choi D.W., Behrens M.M. J. Neurosci. 22:5452-5461(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF NMDA RECEPTORS AND REGULATON OF NMDA RECEPTOR CHANNEL ACTIVITY.
[10]	"Differential regulation of Pyk2 phosphorylation at Tyr-402 and Tyr-580 in intestinal epithelial cells: roles of calcium, Src, Rho kinase, and the cytoskeleton." Wu S.S., Jacamo R.O., Vong S.K., Rozengurt E. Cell. Signal. 18:1932-1940(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT TYR-402 AND TYR-580, CATALYTIC ACTIVITY.
[11]	"Postsynaptic clustering and activation of Pyk2 by PSD-95." Bartos J.A., Ulrich J.D., Li H., Beazely M.A., Chen Y., Macdonald J.F., Hell J.W. J. Neurosci. 30:449-463(2010) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION, INTERACTION WITH DLG4.
[12]	"PYK2 signaling is required for PDGF-dependent vascular smooth muscle cell proliferation." Perez J., Torres R.A., Rocic P., Cismowski M.J., Weber D.S., Darley-Usmar V.M., Lucchesi P.A. Am. J. Physiol. 301:C242-C251(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"The Pyk2 FERM regulates Pyk2 complex formation and phosphorylation." Riggs D., Yang Z., Kloss J., Loftus J.C. Cell. Signal. 23:288-296(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-402; TYR-579 AND TYR-580, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U69109 mRNA. Translation: AAC52895.1. D45854 mRNA. Translation: BAA08290.1. AF063890 mRNA. Translation: AAC28340.1. BC101921 mRNA. Translation: AAI01922.1.
IPI	IPI00190485. IPI00231556. IPI00231557.
PIR	A57434.
RefSeq	NP_059014.2. NM_017318.2.
UniGene	Rn.11025.
3D structure databases
ProteinModelPortal	P70600.
SMR	P70600. Positions 415-692, 869-999.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-266266.
PTM databases
PhosphoSite	P70600.
Proteomic databases
PaxDb	P70600.
PRIDE	P70600.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000030007; ENSRNOP00000031615; ENSRNOG00000027839. ENSRNOT00000030036; ENSRNOP00000036813; ENSRNOG00000027839.
GeneID	50646.
KEGG	rno:50646.
UCSC	RGD:628758. rat.
Organism-specific databases
CTD	2185.
RGD	628758. Ptk2b.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087791.
HOGENOM	HOG000069938.
HOVERGEN	HBG004018.
InParanoid	P70600.
KO	K05871.
OMA	CKRQMLT.
OrthoDB	EOG4SF956.
Enzyme and pathway databases
BRENDA	2.7.10.2. 5301.
Gene expression databases
ArrayExpress	P70600.
Genevestigator	P70600.
GermOnline	ENSRNOG00000027839. Rattus norvegicus.
Family and domain databases
Gene3D	1.20.80.10. 1 hit.
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_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
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]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1075222.
NextBio	610458.

Entry information

Entry name

FAK2_RAT

Accession

Primary (citable) accession number: P70600
Secondary accession number(s): O88489, Q3T1H4, Q63201

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program