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P70600

- FAK2_RAT

UniProt

P70600 - FAK2_RAT

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Protein

Protein-tyrosine kinase 2-beta

Gene

Ptk2b

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

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

GO - Biological processi

  1. actin filament organization Source: RGD
  2. activation of Janus kinase activity Source: RGD
  3. activation of Rac GTPase activity Source: RGD
  4. angiogenesis Source: RGD
  5. blood vessel endothelial cell migration Source: RGD
  6. bone resorption Source: UniProtKB
  7. cell adhesion Source: RGD
  8. cell differentiation Source: RGD
  9. cell surface receptor signaling pathway Source: UniProtKB
  10. cellular defense response Source: Alzheimers_University_of_Toronto
  11. cellular response to retinoic acid Source: Ensembl
  12. chemokine-mediated signaling pathway Source: UniProtKB
  13. epidermal growth factor receptor signaling pathway Source: RGD
  14. focal adhesion assembly Source: RGD
  15. glial cell proliferation Source: RGD
  16. integrin-mediated signaling pathway Source: UniProtKB
  17. ionotropic glutamate receptor signaling pathway Source: Alzheimers_University_of_Toronto
  18. long-term synaptic potentiation Source: Alzheimers_University_of_Toronto
  19. MAPK cascade Source: RGD
  20. marginal zone B cell differentiation Source: UniProtKB
  21. negative regulation of apoptotic process Source: UniProtKB
  22. negative regulation of bone mineralization Source: UniProtKB
  23. negative regulation of cell proliferation Source: UniProtKB
  24. negative regulation of muscle cell apoptotic process Source: RGD
  25. negative regulation of myeloid cell differentiation Source: Ensembl
  26. negative regulation of neuron apoptotic process Source: Alzheimers_University_of_Toronto
  27. negative regulation of ossification Source: RGD
  28. negative regulation of potassium ion transport Source: Ensembl
  29. neuron projection development Source: RGD
  30. oocyte maturation Source: RGD
  31. peptidyl-tyrosine autophosphorylation Source: Alzheimers_University_of_Toronto
  32. peptidyl-tyrosine phosphorylation Source: Alzheimers_University_of_Toronto
  33. positive regulation of actin filament polymerization Source: UniProtKB
  34. positive regulation of B cell chemotaxis Source: UniProtKB
  35. positive regulation of cell growth Source: RGD
  36. positive regulation of cell-matrix adhesion Source: UniProtKB
  37. positive regulation of cell migration Source: RGD
  38. positive regulation of cell proliferation Source: RGD
  39. positive regulation of cytosolic calcium ion concentration Source: RGD
  40. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  41. positive regulation of excitatory postsynaptic membrane potential Source: Alzheimers_University_of_Toronto
  42. positive regulation of JNK cascade Source: UniProtKB
  43. positive regulation of JUN kinase activity Source: RGD
  44. positive regulation of neuron projection development Source: Ensembl
  45. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  46. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  47. positive regulation of protein kinase activity Source: UniProtKB
  48. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  49. positive regulation of reactive oxygen species metabolic process Source: RGD
  50. positive regulation of synaptic transmission, glutamatergic Source: Alzheimers_University_of_Toronto
  51. positive regulation of translation Source: RGD
  52. regulation of actin cytoskeleton reorganization Source: UniProtKB
  53. regulation of cell adhesion Source: UniProtKB
  54. regulation of cell shape Source: UniProtKB
  55. regulation of establishment of cell polarity Source: UniProtKB
  56. regulation of inositol trisphosphate biosynthetic process Source: UniProtKB
  57. regulation of macrophage chemotaxis Source: UniProtKB
  58. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Alzheimers_University_of_Toronto
  59. regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
  60. response to calcium ion Source: RGD
  61. response to cAMP Source: RGD
  62. response to cocaine Source: RGD
  63. response to drug Source: RGD
  64. response to ethanol Source: RGD
  65. response to glucose Source: RGD
  66. response to hormone Source: RGD
  67. response to hydrogen peroxide Source: RGD
  68. response to hypoxia Source: RGD
  69. response to immobilization stress Source: RGD
  70. response to lithium ion Source: RGD
  71. response to mechanical stimulus Source: RGD
  72. response to organonitrogen compound Source: RGD
  73. response to osmotic stress Source: RGD
  74. response to reactive oxygen species Source: RGD
  75. signal complex assembly Source: InterPro
  76. sprouting angiogenesis Source: UniProtKB
  77. stress fiber assembly Source: RGD
  78. tumor necrosis factor-mediated signaling pathway Source: Ensembl
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. 5301.

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
Gene namesi
Name:Ptk2b
Synonyms:Fak2, Pyk2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 15

Organism-specific databases

RGDi628758. Ptk2b.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmperinuclear region By similarity. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. 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).By similarity
Isoform 2 : Cell junctionfocal adhesion
Note: Localizes to focal adhesions, but not isoform 1 and isoform 3.

GO - Cellular componenti

  1. apical dendrite Source: Alzheimers_University_of_Toronto
  2. axon Source: RGD
  3. cell body Source: Alzheimers_University_of_Toronto
  4. cell cortex Source: RGD
  5. dendrite Source: Alzheimers_University_of_Toronto
  6. focal adhesion Source: RGD
  7. growth cone Source: Alzheimers_University_of_Toronto
  8. lamellipodium Source: UniProtKB
  9. membrane raft Source: RGD
  10. neuronal cell body Source: Alzheimers_University_of_Toronto
  11. N-methyl-D-aspartate selective glutamate receptor complex Source: Alzheimers_University_of_Toronto
  12. nucleus Source: RGD
  13. perinuclear region of cytoplasm Source: RGD
  14. postsynaptic density Source: Alzheimers_University_of_Toronto
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10091009Protein-tyrosine kinase 2-betaPRO_0000088083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei399 – 3991PhosphoserineBy similarity
Modified residuei402 – 4021Phosphotyrosine; by autocatalysis2 Publications
Modified residuei440 – 4401PhosphotyrosineBy similarity
Modified residuei579 – 5791Phosphotyrosine; by SRC, LYN and LCK1 Publication
Modified residuei580 – 5801Phosphotyrosine; by SRC, LYN and LCK2 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 – 8811PhosphotyrosineBy similarity

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

PaxDbiP70600.
PRIDEiP70600.

PTM databases

PhosphoSiteiP70600.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

GenevestigatoriP70600.

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 LPXN and PTPN12 (By similarity). Interacts with SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts with ARHGAP10.By similarity4 Publications

Protein-protein interaction databases

BioGridi248405. 4 interactions.
MINTiMINT-266266.

Structurei

3D structure databases

ProteinModelPortaliP70600.
SMRiP70600. Positions 415-692, 869-999.
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 TGFB1I1Add
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.
InParanoidiP70600.
KOiK05871.
OMAiQMLTASH.
OrthoDBiEOG7ZSHSB.
PhylomeDBiP70600.
TreeFamiTF316643.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P70600) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSGVSEPLSR VKVGTLRPPE 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
EFKQIRSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG
360 370 380 390 400
YCRLQGEHKG SLIIHAKKDG EKRNSLPQIP TLNLESRRSH LSESCSIESD
410 420 430 440 450
IYAEIPDETL RRPGGPQYGV AREDVVLNRI LGEGFFGEVY EGVYTNHKGE
460 470 480 490 500
KINVAVKTCK KDCTLDNKEK FMSEAVIMKN LDHPHIVKLI GIIEEEPTWI
510 520 530 540 550
VMELYPYGEL GHYLERNKNS LKVPTLVLYA 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 DIYQMERDIA IEQERNARYR
710 720 730 740 750
PPKILEPTAF QEPPPKPSRP KYKHPPQTNL LAPKLQFQVP EGLCASSPTL
760 770 780 790 800
TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR EEDFIRPSSR EEAQQLWEAE
810 820 830 840 850
KIKMRQVLDR QQKQMVEDSQ WLRREERCLD PMVYMNDKSP LTPEKEAGYT
860 870 880 890 900
EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLSQ
910 920 930 940 950
LPPEEYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL
960 970 980 990 1000
AELINKMRLA QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV

ANLAHPPAE
Length:1,009
Mass (Da):115,784
Last modified:February 1, 1997 - v1
Checksum:iD435A475BCA49E9B
GO
Isoform 2 (identifier: P70600-2) [UniParc]FASTAAdd to Basket

Also known as: PRNK

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

Show »
Length:238
Mass (Da):26,808
Checksum:i223D384D7CE2F9F4
GO
Isoform 3 (identifier: P70600-3) [UniParc]FASTAAdd to Basket

Also known as: PYK2s

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

Show »
Length:967
Mass (Da):111,093
Checksum:iCE6F8A2223E69167
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051E → A in BAA08290. (PubMed:7673154)Curated
Sequence conflicti807 – 8071V → F in AAC28340. (PubMed:9645946)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 771771Missing in isoform 2. 1 PublicationVSP_004982Add
BLAST
Alternative sequencei739 – 78042Missing in isoform 3. 1 PublicationVSP_004984Add
BLAST
Alternative sequencei772 – 7809NVFKRHSMR → MGLIVLSSQ in isoform 2. 1 PublicationVSP_004983

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69109 mRNA. Translation: AAC52895.1.
D45854 mRNA. Translation: BAA08290.1.
AF063890 mRNA. Translation: AAC28340.1.
BC101921 mRNA. Translation: AAI01922.1.
PIRiA57434.
RefSeqiNP_059014.2. NM_017318.2. [P70600-1]
XP_006252205.1. XM_006252143.2. [P70600-1]
XP_006252206.1. XM_006252144.2. [P70600-1]
XP_006252207.1. XM_006252145.2. [P70600-3]
UniGeneiRn.11025.

Genome annotation databases

EnsembliENSRNOT00000030007; ENSRNOP00000031615; ENSRNOG00000027839. [P70600-1]
ENSRNOT00000030036; ENSRNOP00000036813; ENSRNOG00000027839. [P70600-3]
GeneIDi50646.
KEGGirno:50646.
UCSCiRGD:628758. rat. [P70600-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69109 mRNA. Translation: AAC52895.1 .
D45854 mRNA. Translation: BAA08290.1 .
AF063890 mRNA. Translation: AAC28340.1 .
BC101921 mRNA. Translation: AAI01922.1 .
PIRi A57434.
RefSeqi NP_059014.2. NM_017318.2. [P70600-1 ]
XP_006252205.1. XM_006252143.2. [P70600-1 ]
XP_006252206.1. XM_006252144.2. [P70600-1 ]
XP_006252207.1. XM_006252145.2. [P70600-3 ]
UniGenei Rn.11025.

3D structure databases

ProteinModelPortali P70600.
SMRi P70600. Positions 415-692, 869-999.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248405. 4 interactions.
MINTi MINT-266266.

Chemistry

ChEMBLi CHEMBL1075222.

PTM databases

PhosphoSitei P70600.

Proteomic databases

PaxDbi P70600.
PRIDEi P70600.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000030007 ; ENSRNOP00000031615 ; ENSRNOG00000027839 . [P70600-1 ]
ENSRNOT00000030036 ; ENSRNOP00000036813 ; ENSRNOG00000027839 . [P70600-3 ]
GeneIDi 50646.
KEGGi rno:50646.
UCSCi RGD:628758. rat. [P70600-1 ]

Organism-specific databases

CTDi 2185.
RGDi 628758. Ptk2b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118799.
HOGENOMi HOG000069938.
HOVERGENi HBG004018.
InParanoidi P70600.
KOi K05871.
OMAi QMLTASH.
OrthoDBi EOG7ZSHSB.
PhylomeDBi P70600.
TreeFami TF316643.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 5301.

Miscellaneous databases

NextBioi 610458.
PROi P70600.

Gene expression databases

Genevestigatori P70600.

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. "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. 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.

Entry informationi

Entry nameiFAK2_RAT
AccessioniPrimary (citable) accession number: P70600
Secondary accession number(s): O88489, Q3T1H4, Q63201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 145 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3