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P70600 (FAK2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1009 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Cytoplasmperinuclear region By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionlamellipodium By similarity. Cytoplasmcell 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 junctionfocal 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 processAdaptive immunity
Angiogenesis
Immunity
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from mutant phenotype PubMed 15096502. Source: RGD

actin filament organization

Inferred from mutant phenotype PubMed 17127746. 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

angiogenesis

Inferred from mutant phenotype Ref.8. 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

cell adhesion

Inferred from mutant phenotype Ref.8. Source: RGD

cell differentiation

Inferred from expression pattern PubMed 10964954. Source: RGD

cell surface receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

chemokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

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 apoptotic process

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: Ensembl

negative regulation of ossification

Inferred from mutant phenotype PubMed 17537919. Source: RGD

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from mutant phenotype PubMed 10980697. Source: RGD

oocyte maturation

Inferred from mutant phenotype PubMed 17127746. Source: RGD

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 14585963. 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: Ensembl

positive regulation of cell growth

Inferred from mutant phenotype PubMed 15158121. Source: RGD

positive regulation of cell migration

Inferred from mutant phenotype PubMed 16945503. 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 cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 11739373. Source: RGD

positive regulation of endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein 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: Ensembl

regulation of cGMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

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: Ensembl

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

Inferred from expression pattern PubMed 11463795. Source: RGD

response to hormone

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 immobilization stress

Inferred from expression pattern PubMed 12946883. 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 organonitrogen compound

Inferred from expression pattern PubMed 16877402. Source: RGD

response to osmotic stress

Inferred from expression pattern PubMed 11530010. Source: RGD

response to reactive oxygen species

Inferred from expression pattern PubMed 15203192. 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: Ensembl

vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

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_function3-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

protein complex binding

Inferred from physical interaction PubMed 10708762. Source: RGD

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10091009Protein-tyrosine kinase 2-beta
PRO_0000088083

Regions

Domain39 – 359321FERM
Domain425 – 683259Protein kinase
Nucleotide binding431 – 4399ATP By similarity
Nucleotide binding503 – 5097ATP By similarity
Region801 – 1009209Interaction with TGFB1I1
Region868 – 1009142Focal adhesion targeting (FAT)
Compositional bias701 – 76767Pro-rich
Compositional bias831 – 86939Pro-rich

Sites

Active site5491Proton acceptor By similarity
Binding site4571ATP By similarity

Amino acid modifications

Modified residue3611Phosphoserine By similarity
Modified residue3751Phosphoserine By similarity
Modified residue3991Phosphoserine By similarity
Modified residue4021Phosphotyrosine; by autocatalysis Ref.10 Ref.13
Modified residue4401Phosphotyrosine By similarity
Modified residue5791Phosphotyrosine; by SRC, LYN and LCK Ref.13
Modified residue5801Phosphotyrosine; by SRC, LYN and LCK Ref.10 Ref.13
Modified residue7221Phosphotyrosine By similarity
Modified residue7621Phosphoserine By similarity
Modified residue7651Phosphothreonine By similarity
Modified residue8341Phosphotyrosine By similarity
Modified residue8391Phosphoserine By similarity
Modified residue8421Phosphothreonine By similarity
Modified residue8491Phosphotyrosine By similarity
Modified residue8661Phosphoserine By similarity
Modified residue8811Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 771771Missing in isoform 2.
VSP_004982
Alternative sequence739 – 78042Missing in isoform 3.
VSP_004984
Alternative sequence772 – 7809NVFKRHSMR → MGLIVLSSQ in isoform 2.
VSP_004983

Experimental info

Sequence conflict2051E → A in BAA08290. Ref.2
Sequence conflict8071V → F in AAC28340. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: D435A475BCA49E9B

FASTA1,009115,784
        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 

« Hide

Isoform 2 (PRNK) [UniParc].

Checksum: 223D384D7CE2F9F4
Show »

FASTA23826,808
Isoform 3 (PYK2s) [UniParc].

Checksum: CE6F8A2223E69167
Show »

FASTA967111,093

References

« Hide '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.
PIRA57434.
RefSeqNP_059014.2. NM_017318.2.
XP_006252205.1. XM_006252143.1.
XP_006252206.1. XM_006252144.1.
XP_006252207.1. XM_006252145.1.
UniGeneRn.11025.

3D structure databases

ProteinModelPortalP70600.
SMRP70600. Positions 415-692, 869-999.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248405. 4 interactions.
MINTMINT-266266.

Chemistry

ChEMBLCHEMBL1075222.

PTM databases

PhosphoSiteP70600.

Proteomic databases

PaxDbP70600.
PRIDEP70600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000030007; ENSRNOP00000031615; ENSRNOG00000027839. [P70600-1]
ENSRNOT00000030036; ENSRNOP00000036813; ENSRNOG00000027839. [P70600-3]
GeneID50646.
KEGGrno:50646.
UCSCRGD:628758. rat. [P70600-1]

Organism-specific databases

CTD2185.
RGD628758. Ptk2b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115459.
HOGENOMHOG000069938.
HOVERGENHBG004018.
InParanoidP70600.
KOK05871.
OMAQFRKMIQ.
OrthoDBEOG7ZSHSB.
PhylomeDBP70600.
TreeFamTF316643.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.

Gene expression databases

GenevestigatorP70600.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
InterProIPR019749. 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio610458.
PROP70600.

Entry information

Entry nameFAK2_RAT
AccessionPrimary (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 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families