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Q9QVP9

- FAK2_MOUSE

UniProt

Q9QVP9 - FAK2_MOUSE

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Protein

Protein-tyrosine kinase 2-beta

Gene

Ptk2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

Enzyme regulationi

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei457 – 4571ATPPROSITE-ProRule annotation
Active sitei549 – 5491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi431 – 4399ATPPROSITE-ProRule annotation
Nucleotide bindingi503 – 5097ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: Alzheimers_University_of_Toronto
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. protein kinase activity Source: MGI
  5. signal transducer activity Source: InterPro

GO - Biological processi

  1. bone resorption Source: UniProtKB
  2. cell surface receptor signaling pathway Source: UniProtKB
  3. cellular defense response Source: Alzheimers_University_of_Toronto
  4. chemokine-mediated signaling pathway Source: UniProtKB
  5. integrin-mediated signaling pathway Source: UniProtKB
  6. ionotropic glutamate receptor signaling pathway Source: Alzheimers_University_of_Toronto
  7. long-term synaptic potentiation Source: Alzheimers_University_of_Toronto
  8. marginal zone B cell differentiation Source: UniProtKB
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of bone mineralization Source: UniProtKB
  11. negative regulation of cell proliferation Source: UniProtKB
  12. negative regulation of neuron apoptotic process Source: Alzheimers_University_of_Toronto
  13. peptidyl-tyrosine autophosphorylation Source: Alzheimers_University_of_Toronto
  14. peptidyl-tyrosine phosphorylation Source: UniProtKB
  15. positive regulation of actin filament polymerization Source: UniProtKB
  16. positive regulation of angiogenesis Source: UniProtKB
  17. positive regulation of B cell chemotaxis Source: UniProtKB
  18. positive regulation of cell-matrix adhesion Source: UniProtKB
  19. positive regulation of cell proliferation Source: UniProtKB
  20. positive regulation of endothelial cell migration Source: UniProtKB
  21. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  22. positive regulation of excitatory postsynaptic membrane potential Source: Alzheimers_University_of_Toronto
  23. positive regulation of JNK cascade Source: UniProtKB
  24. positive regulation of nitric-oxide synthase activity Source: UniProtKB
  25. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  26. positive regulation of protein kinase activity Source: UniProtKB
  27. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  28. positive regulation of synaptic transmission, glutamatergic Source: Alzheimers_University_of_Toronto
  29. protein phosphorylation Source: MGI
  30. regulation of actin cytoskeleton reorganization Source: UniProtKB
  31. regulation of calcium-mediated signaling Source: UniProtKB
  32. regulation of cell adhesion Source: UniProtKB
  33. regulation of cell shape Source: UniProtKB
  34. regulation of cGMP biosynthetic process Source: UniProtKB
  35. regulation of cGMP-mediated signaling Source: UniProtKB
  36. regulation of establishment of cell polarity Source: UniProtKB
  37. regulation of inositol trisphosphate biosynthetic process Source: UniProtKB
  38. regulation of macrophage chemotaxis Source: UniProtKB
  39. regulation of nitric oxide biosynthetic process Source: UniProtKB
  40. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Alzheimers_University_of_Toronto
  41. regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
  42. signal complex assembly Source: InterPro
  43. sprouting angiogenesis Source: UniProtKB
  44. vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Angiogenesis, Immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_215628. Signal regulatory protein (SIRP) family interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_261365. Interleukin-2 signaling.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ptk2b
Synonyms:Fak2, Pyk2, Raftk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:104908. Ptk2b.

Subcellular locationi

Cytoplasm. Cytoplasmperinuclear region By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionfocal adhesion. Cell projectionlamellipodium By similarity. Cytoplasmcell 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.By similarity

GO - Cellular componenti

  1. apical dendrite Source: Alzheimers_University_of_Toronto
  2. cell body Source: Alzheimers_University_of_Toronto
  3. cytoplasm Source: UniProtKB-KW
  4. dendrite Source: Alzheimers_University_of_Toronto
  5. focal adhesion Source: InterPro
  6. growth cone Source: Alzheimers_University_of_Toronto
  7. lamellipodium Source: UniProtKB
  8. neuronal cell body Source: Alzheimers_University_of_Toronto
  9. N-methyl-D-aspartate selective glutamate receptor complex Source: Alzheimers_University_of_Toronto
  10. nucleus Source: UniProtKB
  11. postsynaptic density Source: Alzheimers_University_of_Toronto
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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 polulations in bone marrow, lymph nodes and blood, but lack marginal zone B-cells in the spleen.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi402 – 4021Y → A: Loss of phosphorylation and interaction with SRC, and inhibition of bone resorption. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10091009Protein-tyrosine kinase 2-betaPRO_0000088082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611PhosphoserineBy similarity
Modified residuei375 – 3751Phosphoserine1 Publication
Modified residuei399 – 3991PhosphoserineBy similarity
Modified residuei402 – 4021Phosphotyrosine; by autocatalysis6 Publications
Modified residuei440 – 4401Phosphotyrosine
Modified residuei579 – 5791Phosphotyrosine; by SRC, LYN and LCK2 Publications
Modified residuei580 – 5801Phosphotyrosine; by SRC, LYN and LCK3 Publications
Modified residuei722 – 7221PhosphotyrosineBy similarity
Modified residuei762 – 7621PhosphoserineBy similarity
Modified residuei765 – 7651PhosphothreonineBy similarity
Modified residuei834 – 8341PhosphotyrosineBy similarity
Modified residuei839 – 8391PhosphoserineBy similarity
Modified residuei842 – 8421PhosphothreonineBy similarity
Modified residuei849 – 8491PhosphotyrosineBy similarity
Modified residuei866 – 8661PhosphoserineBy similarity
Modified residuei881 – 8811Phosphotyrosine2 Publications

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QVP9.
PaxDbiQ9QVP9.
PRIDEiQ9QVP9.

PTM databases

PhosphoSiteiQ9QVP9.

Expressioni

Gene expression databases

CleanExiMM_PTK2B.
ExpressionAtlasiQ9QVP9. baseline and differential.
GenevestigatoriQ9QVP9.

Interactioni

Subunit structurei

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. Interacts with SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts with ARHGAP10.11 Publications

Protein-protein interaction databases

IntActiQ9QVP9. 4 interactions.
MINTiMINT-266339.

Structurei

3D structure databases

ProteinModelPortaliQ9QVP9.
SMRiQ9QVP9. Positions 21-732, 867-1007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 359321FERMPROSITE-ProRule annotationAdd
BLAST
Domaini425 – 683259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni801 – 1009209Interaction with TGFB1I1By similarityAdd
BLAST
Regioni868 – 1009142Focal adhesion targeting (FAT)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi701 – 76767Pro-richAdd
BLAST
Compositional biasi831 – 86939Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.PROSITE-ProRule annotation
Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000069938.
HOVERGENiHBG004018.
InParanoidiQ9QVP9.
KOiK05871.
OMAiQMLTASH.
OrthoDBiEOG7ZSHSB.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR019749. 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.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
ProDomiPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QVP9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGVSEPLSR VKVGTLRRPE GPPEPMVVVP VDVEKEDVRI LKVCFYSNSF
60 70 80 90 100
NPGKNFKLVK CTVQTEIQEI ITSILLSGRI GPNIQLAECY GLRLKHMKSD
110 120 130 140 150
EIHWLHPQMT VGEVQDKYEC LHVEAEWRYD LQIRYLPEDF MESLKEDRTT
160 170 180 190 200
LLYFYQQLRN DYMQRYASKV SEGMALQLGC LELRRFFKDM PHNALDKKSN
210 220 230 240 250
FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS LREEECVMKF
260 270 280 290 300
FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDTKPTCLA
310 320 330 340 350
EFKQIKSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG
360 370 380 390 400
YCRLQGEHKG SLIMHAKKDG EKRNSLPQIP TLNLEARRSH LSESCSIESD
410 420 430 440 450
IYAEIPDETL RRPGGPQYGV AREEVVLNRI LGEGFFGEVY EGVYTNHKGE
460 470 480 490 500
KINVAVKTCK KDCTQDNKEK FMSEAVIMKN LDHPHIVKLI GIIEEEPTWI
510 520 530 540 550
IMELYPYGEL GHYLERNKNS LKVPTLVLYT LQICKAMAYL ESINCVHRDI
560 570 580 590 600
AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR
610 620 630 640 650
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPELC
660 670 680 690 700
PPVLYTLMTR CWDYDPSDRP RFTELVCSLS DIYQMEKDIA IEQERNARYR
710 720 730 740 750
PPKILEPTTF QEPPPKPSRP KYRPPPQTNL LAPKLQFQVP EGLCASSPTL
760 770 780 790 800
TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR EEDFIRPSSR EEAQQLWEAE
810 820 830 840 850
KIKMKQVLER QQKQMVEDSQ WLRREERCLD PMVYMNDKSP LTPEKEAGYT
860 870 880 890 900
EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLGQ
910 920 930 940 950
LPPEDYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL
960 970 980 990 1000
AELINKMKLA QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV

ANLAHPPAE
Length:1,009
Mass (Da):115,794
Last modified:October 3, 2012 - v2
Checksum:iA17C858ECC9990E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061K → R in AAI37705. (PubMed:15489334)Curated
Sequence conflicti306 – 3061K → R in AAI44850. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC126272 Genomic DNA. No translation available.
AC140329 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36001.1.
BC137704 mRNA. Translation: AAI37705.1.
BC144849 mRNA. Translation: AAI44850.1.
CCDSiCCDS49526.1.
RefSeqiNP_001155838.1. NM_001162366.1.
XP_006518789.1. XM_006518726.1.
UniGeneiMm.21613.

Genome annotation databases

EnsembliENSMUST00000022622; ENSMUSP00000022622; ENSMUSG00000059456.
ENSMUST00000178730; ENSMUSP00000137008; ENSMUSG00000059456.
GeneIDi19229.
KEGGimmu:19229.
UCSCiuc011znr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC126272 Genomic DNA. No translation available.
AC140329 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36001.1 .
BC137704 mRNA. Translation: AAI37705.1 .
BC144849 mRNA. Translation: AAI44850.1 .
CCDSi CCDS49526.1.
RefSeqi NP_001155838.1. NM_001162366.1.
XP_006518789.1. XM_006518726.1.
UniGenei Mm.21613.

3D structure databases

ProteinModelPortali Q9QVP9.
SMRi Q9QVP9. Positions 21-732, 867-1007.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9QVP9. 4 interactions.
MINTi MINT-266339.

Chemistry

ChEMBLi CHEMBL1075289.

PTM databases

PhosphoSitei Q9QVP9.

Proteomic databases

MaxQBi Q9QVP9.
PaxDbi Q9QVP9.
PRIDEi Q9QVP9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022622 ; ENSMUSP00000022622 ; ENSMUSG00000059456 .
ENSMUST00000178730 ; ENSMUSP00000137008 ; ENSMUSG00000059456 .
GeneIDi 19229.
KEGGi mmu:19229.
UCSCi uc011znr.1. mouse.

Organism-specific databases

CTDi 2185.
MGIi MGI:104908. Ptk2b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118799.
HOGENOMi HOG000069938.
HOVERGENi HBG004018.
InParanoidi Q9QVP9.
KOi K05871.
OMAi QMLTASH.
OrthoDBi EOG7ZSHSB.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_215628. Signal regulatory protein (SIRP) family interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_261365. Interleukin-2 signaling.

Miscellaneous databases

NextBioi 296032.
PROi Q9QVP9.
SOURCEi Search...

Gene expression databases

CleanExi MM_PTK2B.
ExpressionAtlasi Q9QVP9. baseline and differential.
Genevestigatori Q9QVP9.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
InterProi 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
ProDomi PD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Brain.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 469-479, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PXN.
  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. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRPA.
  9. "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] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B-CELL DIFFERENTIATION; B-CELL CHEMOTAXIS AND IMMUNE RESPONSE.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP10, FUNCTION IN REGULATION OF ARHGAP10 ACTIVITY AND ACTIVATION OF CDC42 AND RHOA.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-402, INTERACTION WITH NPHP1.
  13. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D3C.
  14. "Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast."
    Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A.
    J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPXN AMD PTPN12.
  15. "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] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  16. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BONE RESORPTION, INTERACTION WITH SRC, PHOSPHORYLATION AT TYR-402, MUTAGENESIS OF TYR-402.
  17. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION IN RESPONSE TO FGR.
  18. "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] [Europe PMC] [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.
  19. "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] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  20. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; TYR-579 AND TYR-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  21. Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-402 AND TYR-579, 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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PXN, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
  28. Cited for: FUNCTION IN SPROUTING ANGIOGENESIS.

Entry informationi

Entry nameiFAK2_MOUSE
AccessioniPrimary (citable) accession number: Q9QVP9
Secondary accession number(s): B2RQ16, G3X8V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3