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Q05397

- FAK1_HUMAN

UniProt

Q05397 - FAK1_HUMAN

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Protein

Focal adhesion kinase 1

Gene

PTK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. 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 the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.23 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-562,271.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei454 – 4541ATP1 PublicationPROSITE-ProRule annotation
Active sitei546 – 5461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi428 – 4347ATP1 PublicationPROSITE-ProRule annotation
Nucleotide bindingi500 – 5023ATP1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. actin binding Source: BHF-UCL
  2. ATP binding Source: UniProtKB-KW
  3. JUN kinase binding Source: BHF-UCL
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  5. protein kinase activity Source: Reactome
  6. protein kinase binding Source: UniProtKB
  7. SH2 domain binding Source: UniProtKB
  8. signal transducer activity Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. apoptotic process Source: Reactome
  3. axon guidance Source: UniProtKB
  4. blood coagulation Source: Reactome
  5. cell motility Source: UniProtKB
  6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  7. central nervous system neuron axonogenesis Source: Ensembl
  8. embryo development Source: UniProtKB
  9. endothelial cell migration Source: Ensembl
  10. ephrin receptor signaling pathway Source: UniProtKB
  11. establishment of cell polarity Source: UniProtKB
  12. establishment of nucleus localization Source: Ensembl
  13. extracellular matrix organization Source: Ensembl
  14. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  15. growth hormone receptor signaling pathway Source: BHF-UCL
  16. heart morphogenesis Source: UniProtKB
  17. innate immune response Source: Reactome
  18. integrin-mediated signaling pathway Source: UniProtKB
  19. microtubule cytoskeleton organization Source: Ensembl
  20. negative regulation of anoikis Source: UniProtKB
  21. negative regulation of apoptotic process Source: UniProtKB
  22. negative regulation of axonogenesis Source: Ensembl
  23. negative regulation of cell-cell adhesion Source: BHF-UCL
  24. negative regulation of organ growth Source: Ensembl
  25. negative regulation of synapse assembly Source: Ensembl
  26. netrin-activated signaling pathway Source: UniProtKB
  27. neuron migration Source: Ensembl
  28. peptidyl-tyrosine phosphorylation Source: UniProtKB
  29. placenta development Source: UniProtKB
  30. platelet activation Source: Reactome
  31. positive regulation of cell migration Source: UniProtKB
  32. positive regulation of cell proliferation Source: UniProtKB
  33. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  34. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  35. positive regulation of protein kinase activity Source: UniProtKB
  36. positive regulation of protein kinase B signaling Source: UniProtKB
  37. positive regulation of protein phosphorylation Source: UniProtKB
  38. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  39. protein autophosphorylation Source: UniProtKB
  40. regulation of cell adhesion mediated by integrin Source: UniProtKB
  41. regulation of cell proliferation Source: UniProtKB
  42. regulation of cell shape Source: UniProtKB
  43. regulation of cytoskeleton organization Source: UniProtKB
  44. regulation of endothelial cell migration Source: UniProtKB
  45. regulation of focal adhesion assembly Source: UniProtKB
  46. regulation of osteoblast differentiation Source: UniProtKB
  47. regulation of Rho GTPase activity Source: UniProtKB
  48. signal complex assembly Source: InterPro
  49. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  50. vasculogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_22351. DCC mediated attractive signaling.
REACT_22384. Netrin mediated repulsion signals.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinkiQ05397.

Names & Taxonomyi

Protein namesi
Recommended name:
Focal adhesion kinase 1 (EC:2.7.10.2)
Short name:
FADK 1
Alternative name(s):
Focal adhesion kinase-related nonkinase
Short name:
FRNK
Protein phosphatase 1 regulatory subunit 71
Short name:
PPP1R71
Protein-tyrosine kinase 2
p125FAK
pp125FAK
Gene namesi
Name:PTK2
Synonyms:FAK, FAK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9611. PTK2.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cytoskeleton Source: ProtInc
  3. cytosol Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. lamellipodium Source: Ensembl
  6. nucleus Source: UniProtKB
  7. stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi397 – 3971Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. 1 Publication
Mutagenesisi928 – 9281V → G: Loss of interaction with TGFB1I1. 1 Publication
Mutagenesisi1034 – 10341L → S: Loss of interaction with TGFB1I1. 1 Publication

Organism-specific databases

PharmGKBiPA33955.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 10521051Focal adhesion kinase 1PRO_0000088077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei5 – 51Phosphotyrosine1 Publication
Modified residuei13 – 131Phosphothreonine2 Publications
Modified residuei29 – 291Phosphoserine2 Publications
Cross-linki152 – 152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei397 – 3971Phosphotyrosine; by autocatalysis7 Publications
Modified residuei407 – 4071Phosphotyrosine2 Publications
Modified residuei570 – 5701Phosphotyrosine1 Publication
Modified residuei576 – 5761Phosphotyrosine; by RET and SRC3 Publications
Modified residuei577 – 5771Phosphotyrosine; by RET and SRC3 Publications
Modified residuei580 – 5801Phosphoserine1 Publication
Modified residuei722 – 7221Phosphoserine1 Publication
Modified residuei732 – 7321Phosphoserine; by CDK5By similarity
Modified residuei861 – 8611Phosphotyrosine3 Publications
Modified residuei887 – 8871Phosphoserine1 Publication
Modified residuei910 – 9101Phosphoserine4 Publications
Modified residuei914 – 9141Phosphothreonine1 Publication
Modified residuei925 – 9251Phosphotyrosine2 Publications

Post-translational modificationi

Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21.11 Publications
Sumoylated; this enhances autophosphorylation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ05397.
PaxDbiQ05397.
PRIDEiQ05397.

PTM databases

PhosphoSiteiQ05397.

Miscellaneous databases

PMAP-CutDBQ05397.

Expressioni

Tissue specificityi

Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous.4 Publications

Developmental stagei

Isoform 6 is detected in cultured cells, immediately after seeding and before formation of focal adhesions (at protein level).

Gene expression databases

BgeeiQ05397.
CleanExiHS_PTK2.
ExpressionAtlasiQ05397. baseline and differential.
GenevestigatoriQ05397.

Organism-specific databases

HPAiCAB004036.
HPA001842.

Interactioni

Subunit structurei

Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 (By similarity). Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2. Interacts with CD36.26 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569452EBI-702142,EBI-702093
CRKLP461092EBI-702142,EBI-910
EGFRP005333EBI-702142,EBI-297353
EPHA2P293173EBI-702142,EBI-702104
ERBB2P046262EBI-702142,EBI-641062
FLT1P179482EBI-702142,EBI-1026718
PTPN23Q9H3S74EBI-702142,EBI-724478
PTRH2Q9Y3E52EBI-702142,EBI-1056751
PXNP4902315EBI-702142,EBI-702209
SRCP129317EBI-702142,EBI-621482
SrcP054805EBI-702142,EBI-298680From a different organism.
TGFB1I1O432942EBI-702142,EBI-1051449
Tgfb1i1Q622193EBI-702142,EBI-642844From a different organism.
TNS3Q68CZ23EBI-702142,EBI-1220488
TP53P0463713EBI-702142,EBI-366083

Protein-protein interaction databases

BioGridi111719. 99 interactions.
IntActiQ05397. 58 interactions.
MINTiMINT-92695.
STRINGi9606.ENSP00000341189.

Structurei

Secondary structure

1
1052
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 406
Helixi49 – 513
Beta strandi53 – 586
Helixi64 – 7310
Turni74 – 763
Helixi80 – 823
Beta strandi83 – 897
Beta strandi95 – 984
Helixi104 – 11411
Helixi117 – 1193
Beta strandi120 – 1267
Helixi133 – 1375
Helixi141 – 15818
Helixi165 – 17915
Helixi185 – 1873
Beta strandi188 – 1903
Helixi191 – 1944
Helixi197 – 2015
Turni204 – 2063
Helixi209 – 2146
Turni217 – 2193
Helixi220 – 2289
Helixi229 – 2313
Helixi236 – 24712
Helixi248 – 2503
Beta strandi256 – 2627
Beta strandi264 – 2663
Beta strandi268 – 2758
Turni276 – 2783
Beta strandi279 – 2835
Beta strandi290 – 2945
Helixi296 – 2983
Beta strandi299 – 3068
Beta strandi308 – 3114
Beta strandi314 – 3207
Beta strandi327 – 3337
Helixi334 – 35118
Helixi413 – 4153
Helixi419 – 4213
Beta strandi422 – 4309
Beta strandi432 – 44110
Beta strandi444 – 4463
Beta strandi448 – 4558
Turni457 – 4604
Helixi462 – 4687
Helixi470 – 4767
Beta strandi486 – 4905
Beta strandi492 – 4943
Beta strandi496 – 5005
Helixi507 – 5137
Turni514 – 5174
Helixi520 – 53920
Helixi549 – 5513
Beta strandi552 – 5565
Beta strandi559 – 5624
Helixi565 – 5684
Helixi570 – 5734
Helixi574 – 5763
Helixi586 – 5883
Helixi591 – 5966
Helixi601 – 61616
Turni617 – 6193
Turni622 – 6254
Helixi628 – 6303
Helixi631 – 6366
Helixi649 – 65810
Helixi663 – 6653
Helixi669 – 68416
Helixi685 – 6873
Beta strandi915 – 9173
Helixi923 – 94220
Helixi947 – 9493
Helixi950 – 97122
Helixi972 – 9743
Helixi977 – 9793
Helixi980 – 100627
Turni1007 – 10093
Beta strandi1010 – 10123
Helixi1013 – 104533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K04X-ray1.95A891-1052[»]
1K05X-ray2.90A/B/C891-1052[»]
1MP8X-ray1.60A411-686[»]
1OW6X-ray2.35A/B/C892-1052[»]
1OW7X-ray2.60A/B/C892-1052[»]
1OW8X-ray2.85A/B/C892-1052[»]
2ETMX-ray2.30A/B411-689[»]
2IJMX-ray2.19A/B411-689[»]
2RA7X-ray1.99A921-1048[»]
3B71X-ray2.82A/B/C891-1052[»]
3BZ3X-ray2.20A414-689[»]
3PXKX-ray1.79A/B411-689[»]
3S9OX-ray2.60A/B/C891-1052[»]
4EBVX-ray1.67A411-686[»]
4EBWX-ray2.65A411-686[»]
4GU6X-ray1.95A/B411-689[»]
4GU9X-ray2.40A/B410-686[»]
4I4EX-ray1.55A411-686[»]
4I4FX-ray1.75A411-686[»]
4K8AX-ray2.91A/B410-686[»]
4K9YX-ray2.00A410-686[»]
4KABX-ray2.71A/B410-686[»]
4KAOX-ray2.39A/B410-689[»]
4NY0X-ray2.80A/B/C/D31-405[»]
4Q9SX-ray2.07A411-686[»]
ProteinModelPortaliQ05397.
SMRiQ05397. Positions 34-715, 908-1049.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05397.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 355321FERMPROSITE-ProRule annotationAdd
BLAST
Domaini422 – 680259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni707 – 1052346Interaction with TGFB1I1Add
BLAST
Regioni912 – 1052141Interaction with ARHGEF28By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi712 – 73322Pro-richAdd
BLAST
Compositional biasi863 – 91351Pro-richAdd
BLAST

Domaini

The Pro-rich regions interact with the SH3 domain of CAS family members, such as BCAR1 and NEDD9, and with the GTPase activating protein ARHGAP26.
The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

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.
InParanoidiQ05397.
KOiK05725.
OrthoDBiEOG7ZSHSB.
PhylomeDBiQ05397.
TreeFamiTF316643.

Family and domain databases

InterProiIPR019749. Band_41_domain.
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.
PROSITEiPS00661. FERM_2. 1 hit.
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]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: Q05397) [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
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT
60 70 80 90 100
TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV
110 120 130 140 150
DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190 200
VKSDYMLEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA
460 470 480 490 500
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME
510 520 530 540 550
LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590 600
NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
610 620 630 640 650
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT
660 670 680 690 700
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS
760 770 780 790 800
HGITAMAGSI YPGQASLLDQ TDSWNHRPQE IAMWQPNVED STVLDLRGIG
810 820 830 840 850
QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS
860 870 880 890 900
LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE
910 920 930 940 950
GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY
960 970 980 990 1000
VPMVKEVGLA LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK
1010 1020 1030 1040 1050
MKLAQQYVMT SLQQEYKKQM LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR

PH
Length:1,052
Mass (Da):119,233
Last modified:July 15, 1998 - v2
Checksum:iD8A4C15138AB0243
GO
Isoform 2 (identifier: Q05397-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     834-854: Missing.

Show »
Length:879
Mass (Da):99,358
Checksum:i64783EFF1FF4FCCB
GO
Isoform 3 (identifier: Q05397-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     677-706: STILEEEKAQQEERMRMESRRQATVSWDSG → FQNPAQMLPASGRLPNQPCPERENYSFATF
     707-1052: Missing.

Show »
Length:554
Mass (Da):63,201
Checksum:i3960D6100B580E7D
GO
Isoform 4 (identifier: Q05397-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     579-583: ASKGK → GKKSG
     584-1052: Missing.

Show »
Length:431
Mass (Da):48,967
Checksum:i9C8013A49B83C690
GO
Isoform 5 (identifier: Q05397-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     868-868: D → GKEEKNWAERN
     903-903: K → KPWR

Show »
Length:1,065
Mass (Da):120,900
Checksum:i3FC0C66C4CF858D8
GO
Isoform 6 (identifier: Q05397-6) [UniParc]FASTAAdd to Basket

Also known as: FRNK

The sequence of this isoform differs from the canonical sequence as follows:
     1-692: Missing.

Note: Produced by alternative promoter usage.

Show »
Length:360
Mass (Da):39,874
Checksum:i0BD7ACE4EAEE63C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841R → L in BAG65198. (PubMed:14702039)Curated
Sequence conflicti211 – 2111L → I in BAG65198. (PubMed:14702039)Curated
Sequence conflicti778 – 7781P → S in AAA35819. (PubMed:8422239)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921H → P.1 Publication
VAR_041682
Natural varianti292 – 2921H → Q.1 Publication
VAR_041683
Natural varianti793 – 7931V → A in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041684
Natural varianti1030 – 10301D → E.1 Publication
VAR_041685
Natural varianti1044 – 10441K → E in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041686

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 692692Missing in isoform 6. CuratedVSP_042168Add
BLAST
Alternative sequencei1 – 181181Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_004967Add
BLAST
Alternative sequencei182 – 1898EMRGNALE → MSDYWVVG in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_004968
Alternative sequencei472 – 4721A → ACHYTSLHWNWCRYISDPNV DACPDPRNAE in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_004969
Alternative sequencei579 – 5835ASKGK → GKKSG in isoform 4. 1 PublicationVSP_004971
Alternative sequencei584 – 1052469Missing in isoform 4. 1 PublicationVSP_004972Add
BLAST
Alternative sequencei677 – 70630STILE…SWDSG → FQNPAQMLPASGRLPNQPCP ERENYSFATF in isoform 3. 1 PublicationVSP_004973Add
BLAST
Alternative sequencei707 – 1052346Missing in isoform 3. 1 PublicationVSP_004974Add
BLAST
Alternative sequencei834 – 85421Missing in isoform 2. 1 PublicationVSP_004970Add
BLAST
Alternative sequencei868 – 8681D → GKEEKNWAERN in isoform 5. 1 PublicationVSP_042169
Alternative sequencei903 – 9031K → KPWR in isoform 5. 1 PublicationVSP_042170

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13616 mRNA. Translation: AAA58469.1.
L05186 mRNA. Translation: AAA35819.1.
AK304356 mRNA. Translation: BAG65198.1.
AC067931 Genomic DNA. No translation available.
AC100860 Genomic DNA. No translation available.
AC105009 Genomic DNA. No translation available.
AC105235 Genomic DNA. No translation available.
CCDSiCCDS56557.1. [Q05397-5]
CCDS6381.1. [Q05397-1]
PIRiI53012.
PC1225.
RefSeqiNP_001186578.1. NM_001199649.1. [Q05397-5]
NP_722560.1. NM_153831.3. [Q05397-1]
UniGeneiHs.395482.

Genome annotation databases

EnsembliENST00000340930; ENSP00000341189; ENSG00000169398. [Q05397-5]
ENST00000521059; ENSP00000429474; ENSG00000169398. [Q05397-1]
ENST00000522684; ENSP00000429911; ENSG00000169398. [Q05397-1]
GeneIDi5747.
KEGGihsa:5747.
UCSCiuc003yvq.3. human. [Q05397-2]
uc003yvu.3. human. [Q05397-1]
uc011ljp.2. human. [Q05397-6]
uc011ljr.2. human. [Q05397-5]

Polymorphism databases

DMDMi3183518.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13616 mRNA. Translation: AAA58469.1 .
L05186 mRNA. Translation: AAA35819.1 .
AK304356 mRNA. Translation: BAG65198.1 .
AC067931 Genomic DNA. No translation available.
AC100860 Genomic DNA. No translation available.
AC105009 Genomic DNA. No translation available.
AC105235 Genomic DNA. No translation available.
CCDSi CCDS56557.1. [Q05397-5 ]
CCDS6381.1. [Q05397-1 ]
PIRi I53012.
PC1225.
RefSeqi NP_001186578.1. NM_001199649.1. [Q05397-5 ]
NP_722560.1. NM_153831.3. [Q05397-1 ]
UniGenei Hs.395482.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K04 X-ray 1.95 A 891-1052 [» ]
1K05 X-ray 2.90 A/B/C 891-1052 [» ]
1MP8 X-ray 1.60 A 411-686 [» ]
1OW6 X-ray 2.35 A/B/C 892-1052 [» ]
1OW7 X-ray 2.60 A/B/C 892-1052 [» ]
1OW8 X-ray 2.85 A/B/C 892-1052 [» ]
2ETM X-ray 2.30 A/B 411-689 [» ]
2IJM X-ray 2.19 A/B 411-689 [» ]
2RA7 X-ray 1.99 A 921-1048 [» ]
3B71 X-ray 2.82 A/B/C 891-1052 [» ]
3BZ3 X-ray 2.20 A 414-689 [» ]
3PXK X-ray 1.79 A/B 411-689 [» ]
3S9O X-ray 2.60 A/B/C 891-1052 [» ]
4EBV X-ray 1.67 A 411-686 [» ]
4EBW X-ray 2.65 A 411-686 [» ]
4GU6 X-ray 1.95 A/B 411-689 [» ]
4GU9 X-ray 2.40 A/B 410-686 [» ]
4I4E X-ray 1.55 A 411-686 [» ]
4I4F X-ray 1.75 A 411-686 [» ]
4K8A X-ray 2.91 A/B 410-686 [» ]
4K9Y X-ray 2.00 A 410-686 [» ]
4KAB X-ray 2.71 A/B 410-686 [» ]
4KAO X-ray 2.39 A/B 410-689 [» ]
4NY0 X-ray 2.80 A/B/C/D 31-405 [» ]
4Q9S X-ray 2.07 A 411-686 [» ]
ProteinModelPortali Q05397.
SMRi Q05397. Positions 34-715, 908-1049.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111719. 99 interactions.
IntActi Q05397. 58 interactions.
MINTi MINT-92695.
STRINGi 9606.ENSP00000341189.

Chemistry

BindingDBi Q05397.
ChEMBLi CHEMBL2695.
GuidetoPHARMACOLOGYi 2180.

PTM databases

PhosphoSitei Q05397.

Polymorphism databases

DMDMi 3183518.

Proteomic databases

MaxQBi Q05397.
PaxDbi Q05397.
PRIDEi Q05397.

Protocols and materials databases

DNASUi 5747.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340930 ; ENSP00000341189 ; ENSG00000169398 . [Q05397-5 ]
ENST00000521059 ; ENSP00000429474 ; ENSG00000169398 . [Q05397-1 ]
ENST00000522684 ; ENSP00000429911 ; ENSG00000169398 . [Q05397-1 ]
GeneIDi 5747.
KEGGi hsa:5747.
UCSCi uc003yvq.3. human. [Q05397-2 ]
uc003yvu.3. human. [Q05397-1 ]
uc011ljp.2. human. [Q05397-6 ]
uc011ljr.2. human. [Q05397-5 ]

Organism-specific databases

CTDi 5747.
GeneCardsi GC08M141667.
HGNCi HGNC:9611. PTK2.
HPAi CAB004036.
HPA001842.
MIMi 600758. gene.
neXtProti NX_Q05397.
PharmGKBi PA33955.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118799.
HOGENOMi HOG000069938.
HOVERGENi HBG004018.
InParanoidi Q05397.
KOi K05725.
OrthoDBi EOG7ZSHSB.
PhylomeDBi Q05397.
TreeFami TF316643.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_22351. DCC mediated attractive signaling.
REACT_22384. Netrin mediated repulsion signals.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinki Q05397.

Miscellaneous databases

ChiTaRSi PTK2. human.
EvolutionaryTracei Q05397.
GeneWikii PTK2.
GenomeRNAii 5747.
NextBioi 22380.
PMAP-CutDB Q05397.
PROi Q05397.
SOURCEi Search...

Gene expression databases

Bgeei Q05397.
CleanExi HS_PTK2.
ExpressionAtlasi Q05397. baseline and differential.
Genevestigatori Q05397.

Family and domain databases

InterProi IPR019749. Band_41_domain.
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 PS00661. FERM_2. 1 hit.
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. "Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK."
    Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A., Kanner S.B.
    DNA Cell Biol. 12:823-830(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: T-cell.
  2. "Expression of an N-terminally truncated form of human focal adhesion kinase in brain."
    Andre E., Becker-Andre M.
    Biochem. Biophys. Res. Commun. 190:140-147(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Trachea.
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419; 468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND 1003-1042, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  6. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
    Lee S.-T., Strunk K.M., Spritz R.A.
    Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, TISSUE SPECIFICITY.
    Tissue: Melanocyte.
  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. "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase."
    Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.
    J. Biol. Chem. 273:26516-26521(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1, MUTAGENESIS OF VAL-928 AND LEU-1034.
  9. "Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
    Miao H., Burnett E., Kinch M., Simon E., Wang B.
    Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION.
  10. "Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
    Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
    Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, INTERACTION WITH BMX.
  11. "Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples."
    Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.
    Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SHC1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1 AND SRC, ROLE IN DISEASE.
  12. "Regulation of focal adhesion kinase by a novel protein inhibitor FIP200."
    Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R., Guan J.L.
    Mol. Biol. Cell 13:3178-3191(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RB1CC1.
  13. "Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein."
    Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.
    Biochem. J. 369:407-416(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, INTERACTION WITH FGR.
  14. "Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway."
    Xia H., Nho R.S., Kahm J., Kleidon J., Henke C.A.
    J. Biol. Chem. 279:33024-33034(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTEGRIN SIGNALING; REGULATION OF APOPTOSIS; REGULATION OF CELL SHAPE AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND AKT1 SIGNALING PATHWAY.
  15. "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: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION AT TYR-407; TYR-397 AND TYR-576.
  16. "Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53."
    Golubovskaya V.M., Finch R., Cance W.G.
    J. Biol. Chem. 280:25008-25021(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH P53/TP53, SUBCELLULAR LOCATION.
  17. "Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase."
    Ezratty E.J., Partridge M.A., Gundersen G.G.
    Nat. Cell Biol. 7:581-590(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FOCAL ADHESION DISASSEMBLY.
  18. "Vascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells."
    Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.
    Cancer Res. 66:1446-1454(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT4.
  19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Expression of FAK-related non-kinase (FRNK) coincides with morphological change in the early stage of cell adhesion."
    Nagoshi Y., Yamamoto G., Irie T., Tachikawa T.
    Med. Mol. Morphol. 39:154-160(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 6, DEVELOPMENTAL STAGE (ISOFORM 6).
  21. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397 AND TYR-861.
  23. Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397.
  24. "Activation of FAK is necessary for the osteogenic differentiation of human mesenchymal stem cells on laminin-5."
    Salasznyk R.M., Klees R.F., Boskey A., Plopper G.E.
    J. Cell. Biochem. 100:499-514(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION.
  25. "Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo."
    Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T., Jackson D., de Groot J., Yung W.K.
    Mol. Cancer Ther. 6:1357-1367(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397.
  26. "The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
    Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
    Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LPXN.
  27. "Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
    Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
    J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BMX.
  28. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASS4.
  29. "Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation."
    Lim S.T., Chen X.L., Lim Y., Hanson D.A., Vo T.T., Howerton K., Larocque N., Fisher S.J., Schlaepfer D.D., Ilic D.
    Mol. Cell 29:9-22(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL SURVIVAL, SUBCELLULAR LOCATION.
  30. Cited for: INTERACTION WITH ESR1; PIK3R1 AND/OR PIK3R2 AND SRC.
  31. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-887 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes."
    Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G., Oh E.S., Buday L., Kim S.H., Lee J.W.
    Biochim. Biophys. Acta 1793:781-791(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925, IDENTIFICATION IN A COMPLEX WITH CTTN AND FER.
  35. "Paxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion."
    Sachdev S., Bu Y., Gelman I.H.
    BMC Cancer 9:12-12(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN.
  36. "STEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells."
    Tamura T., Chiba J.
    Int. J. Mol. Med. 24:599-604(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STEAP4.
  37. "Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling."
    Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F., Giancotti F.G.
    J. Clin. Invest. 119:252-266(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF BCAR1, ROLE IN DISEASE.
  38. "EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
    Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
    J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHA1.
  39. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5; THR-13; SER-29; TYR-397; TYR-570; SER-580 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models."
    Sun H., Pisle S., Gardner E.R., Figg W.D.
    Cancer Biol. Ther. 10:38-43(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN DISEASE, ENZYME REGULATION.
  41. "LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin."
    Tanaka T., Moriwaki K., Murata S., Miyasaka M.
    Cancer Sci. 101:363-368(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPXN.
  42. "Downregulation of FAK-related non-kinase mediates the migratory phenotype of human fibrotic lung fibroblasts."
    Cai G.Q., Zheng A., Tang Q., White E.S., Chou C.F., Gladson C.L., Olman M.A., Ding Q.
    Exp. Cell Res. 316:1600-1609(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 6), TISSUE SPECIFICITY.
  43. Cited for: INTERACTION WITH ZFYVE21, DEPHOSPHORYLATION AT TYR-397.
  44. "CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer."
    Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.
    Nat. Immunol. 11:155-161(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD36.
  45. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND THR-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  46. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  47. "Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism."
    Plaza-Menacho I., Morandi A., Mologni L., Boender P., Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P., McDonald N.Q., Isacke C.M.
    J. Biol. Chem. 286:17292-17302(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
  48. "A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
    Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
    Oncogene 33:1167-1180(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1 ISOFORM 2.
    Tissue: Brain.
  49. Cited for: REVIEW ON SIGNALING AND ON DIRECT PTK2/FAK1 SUBSTRATES.
  50. "Netrin-integrin signaling in epithelial morphogenesis, axon guidance and vascular patterning."
    Nikolopoulos S.N., Giancotti F.G.
    Cell Cycle 4:E131-E135(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN NETRIN SIGNALING.
  51. "Integrin-regulated FAK-Src signaling in normal and cancer cells."
    Mitra S.K., Schlaepfer D.D.
    Curr. Opin. Cell Biol. 18:516-523(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN CELL MIGRATION; FOCAL ADHESION TURNOVER AND ACTIVATION OF SIGNALING PATHWAYS, ROLE IN DISEASE.
  52. "Focal adhesion kinase: an essential kinase in the regulation of cardiovascular functions."
    Vadali K., Cai X., Schaller M.D.
    IUBMB Life 59:709-716(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  53. "FERM control of FAK function: implications for cancer therapy."
    Lim S.T., Mikolon D., Stupack D.G., Schlaepfer D.D.
    Cell Cycle 7:2306-2314(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53 ACTIVITIES, ROLE IN DISEASE, ENZYME REGULATION.
  54. "Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility."
    Tomar A., Schlaepfer D.D.
    Curr. Opin. Cell Biol. 21:676-683(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN REGULATION OF RHO FAMILY GTPASE ACTIVITY.
  55. "Focal adhesion kinase and cancer."
    Golubovskaya V.M., Kweh F.A., Cance W.G.
    Histol. Histopathol. 24:503-510(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON EXPRESSION IN CANCER, ROLE IN DISEASE.
  56. "Focal adhesion kinase and p53 signal transduction pathways in cancer."
    Golubovskaya V.M., Cance W.
    Front. Biosci. 15:901-912(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN REGULATION OF P53/TP53.
  57. "The role of focal adhesion kinase in early development."
    Chatzizacharias N.A., Kouraklis G.P., Theocharis S.E.
    Histol. Histopathol. 25:1039-1055(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN DEVELOPMENT.
  58. "Integrin signaling through FAK in the regulation of mammary stem cells and breast cancer."
    Guan J.L.
    IUBMB Life 62:268-276(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF DOWNSTREAM SIGNALING PATHWAYS.
  59. "Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions."
    Schaller M.D.
    J. Cell Sci. 123:1007-1013(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SIGNALING.
  60. "Focal adhesion kinase: exploring Fak structure to gain insight into function."
    Hall J.E., Fu W., Schaller M.D.
    Int. Rev. Cell Mol. Biol. 288:185-225(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION; SUBUNIT; PHOSPHORYLATION; ENZYME REGULATION AND ROLE IN DISEASE.
  61. "MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
    Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
    J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MISP.
  62. "The structural basis of localization and signaling by the focal adhesion targeting domain."
    Arold S.T., Hoellerer M.K., Noble M.E.
    Structure 10:319-327(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 891-1052, IDENTIFICATION BY MASS SPECTROMETRY.
  63. "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
    Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
    Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 411-686 IN COMPLEX WITH ATP.
  64. "Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain."
    Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., Arold S.T.
    Structure 11:1207-1217(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 892-1052 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
  65. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
  66. "Structural basis for the interaction between focal adhesion kinase and CD4."
    Garron M.L., Arthos J., Guichou J.F., McNally J., Cicala C., Arold S.T.
    J. Mol. Biol. 375:1320-1328(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 891-1052 IN COMPLEX WITH CD4, SUBCELLULAR LOCATION, INTERACTION WITH CD4.
  67. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND GLU-1044.

Entry informationi

Entry nameiFAK1_HUMAN
AccessioniPrimary (citable) accession number: Q05397
Secondary accession number(s): B4E2N6
, F5H4S4, Q14291, Q9UD85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 15, 1998
Last modified: October 29, 2014
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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