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Q00944

- FAK1_CHICK

UniProt

Q00944 - FAK1_CHICK

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Protein
Focal adhesion kinase 1
Gene
PTK2, FAK, FAK1
Organism
Gallus gallus (Chicken)
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, 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), ephrin receptors, 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. Regulates P53/TP53 activity and stability. Phosphorylates SRC; this increases SRC kinase activity. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling.6 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

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 TAE226.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei454 – 4541ATP Inferred
Active sitei546 – 5461Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi428 – 4347ATP Inferred
Nucleotide bindingi500 – 5023ATP Inferred

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. protein binding Source: IntAct
  5. signal transducer activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. signal complex assembly Source: InterPro
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. 1306.
ReactomeiREACT_197606. Regulation of actin dynamics for phagocytic cup formation.
REACT_204997. Netrin mediated repulsion signals.
REACT_207020. DCC mediated attractive signaling.

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
Short name:
p41/p43FRNK
Protein-tyrosine kinase 2
p125FAK
pp125FAK
Gene namesi
Name:PTK2
Synonyms:FAK, FAK1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 2

Subcellular locationi

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus
Note: Constituent of focal adhesions. Detected at microtubules By similarity.1 Publication

GO - Cellular componenti

  1. focal adhesion Source: UniProtKB-SubCell
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi395 – 3951D → A: Abolishes interaction with PIK3R1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10531053Focal adhesion kinase 1
PRO_0000088076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei397 – 3971Phosphotyrosine; by autocatalysis1 Publication
Modified residuei407 – 4071Phosphotyrosine By similarity
Modified residuei576 – 5761Phosphotyrosine; by SRC2 Publications
Modified residuei577 – 5771Phosphotyrosine; by SRC By similarity
Modified residuei863 – 8631Phosphotyrosine1 Publication
Modified residuei911 – 9111Phosphoserine1 Publication
Modified residuei926 – 9261Phosphotyrosine By similarity

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. Isoform 2 is phosphorylated on serine or threonine residues, but apparently not on tyrosine residues.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ00944.
PRIDEiQ00944.

Interactioni

Subunit structurei

Interacts with ARHGAP26, GRB7, DCC, PIK3R1, PXN and SRC. Interacts with the ARP2/3 complex.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-2896409,EBI-2896409
ACTR3P611575EBI-2896409,EBI-351419From a different organism.
METP085815EBI-2896409,EBI-1039152From a different organism.
PXNP490242EBI-2896409,EBI-2896280
SRCP005233EBI-2896409,EBI-848039

Protein-protein interaction databases

BioGridi676665. 2 interactions.
IntActiQ00944. 11 interactions.
MINTiMINT-1517788.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 405
Helixi49 – 513
Beta strandi53 – 586
Helixi64 – 7411
Helixi80 – 823
Beta strandi83 – 897
Beta strandi95 – 984
Beta strandi100 – 1034
Helixi104 – 1129
Helixi117 – 1193
Beta strandi120 – 1267
Helixi133 – 1375
Helixi141 – 15818
Turni159 – 1624
Helixi165 – 17915
Turni180 – 1823
Helixi187 – 1893
Helixi191 – 1999
Turni200 – 2023
Helixi203 – 2053
Helixi209 – 2135
Helixi217 – 22913
Turni230 – 2334
Helixi236 – 24712
Turni248 – 2503
Beta strandi256 – 2627
Beta strandi264 – 2663
Beta strandi268 – 2758
Turni276 – 2783
Beta strandi279 – 2857
Beta strandi290 – 2945
Helixi296 – 2983
Beta strandi299 – 3057
Beta strandi308 – 3103
Beta strandi314 – 3207
Beta strandi327 – 3337
Helixi334 – 35219
Beta strandi398 – 4025
Helixi412 – 4143
Helixi419 – 4213
Beta strandi422 – 4309
Beta strandi432 – 44110
Beta strandi444 – 4463
Beta strandi448 – 4558
Turni457 – 4604
Helixi462 – 47615
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
Beta strandi573 – 5753
Helixi586 – 5883
Helixi591 – 5966
Helixi601 – 61616
Turni617 – 6193
Turni622 – 6254
Helixi628 – 6303
Helixi631 – 6366
Helixi649 – 65810
Helixi663 – 6653
Helixi669 – 68517
Turni919 – 9213
Helixi922 – 94120
Turni942 – 9454
Helixi948 – 97528
Turni978 – 9803
Helixi982 – 100524
Beta strandi1008 – 10125
Helixi1014 – 104734

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTMNMR-A916-1053[»]
1PV3NMR-A920-1053[»]
1QVXNMR-A920-1053[»]
2AEHX-ray2.53A/B31-399[»]
2AL6X-ray2.35A/B31-405[»]
2J0JX-ray2.80A31-686[»]
2J0KX-ray3.00A/B31-686[»]
2J0LX-ray2.30A411-686[»]
2J0MX-ray2.80A31-399[»]
B411-686[»]
2JKKX-ray2.00A411-686[»]
2JKMX-ray2.31A411-686[»]
2JKOX-ray1.65A411-686[»]
2JKQX-ray2.60A411-686[»]
2L6FNMR-A916-1053[»]
2L6GNMR-A916-1053[»]
2L6HNMR-A916-1053[»]
3ZDTX-ray3.15A/B31-405[»]
4BRXX-ray2.05A411-686[»]
4C7TX-ray2.05A411-686[»]
4CYEX-ray3.20A/B31-405[»]
ProteinModelPortaliQ00944.
SMRiQ00944. Positions 33-686, 916-1053.

Miscellaneous databases

EvolutionaryTraceiQ00944.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 355321FERM
Add
BLAST
Domaini422 – 680259Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi712 – 73322Pro-rich
Add
BLAST
Compositional biasi865 – 91450Pro-rich
Add
BLAST

Domaini

The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

Sequence similaritiesi

Contains 1 FERM domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000115459.
HOGENOMiHOG000069938.
HOVERGENiHBG004018.
KOiK05725.
PhylomeDBiQ00944.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: Q00944-1) [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

MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT     50
TWASIIRHGD ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL 100
DMGVSNVREK FELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ 150
VKNDYMLEIA DQVDQEIALK LGCLEIRRSY GEMRGNALEK KSNYEVLEKD 200
VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 250
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ 300
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 350
VNGATQSFII RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI 400
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPAMA 450
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME 500
LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR 550
NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 600
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT 650
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT 700
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS 750
HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE VSAWQPNMED SGTLDVRGMG 800
QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR LSRGSIERED 850
GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN 900
EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE 950
YVPMVKEVGL ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN 1000
KMKLAQQYVM TSLQQEYKKQ MLTAAHALAV DAKNLLDVID QARLKMISQS 1050
RPH 1053
Length:1,053
Mass (Da):119,207
Last modified:February 1, 1994 - v2
Checksum:i8051154219B953B9
GO
Isoform 2 (identifier: Q00944-2) [UniParc]FASTAAdd to Basket

Also known as: FRNK

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

Show »
Length:361
Mass (Da):40,032
Checksum:i61E6AD4B50CCCC49
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 692692Missing in isoform 2.
VSP_042173Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86656 mRNA. Translation: AAA48765.1.
L08402 mRNA. Translation: AAA48766.1.
PIRiA45388.
PC1239.
RefSeqiNP_990766.1. NM_205435.1. [Q00944-1]
UniGeneiGga.15614.

Genome annotation databases

EnsembliENSGALT00000026060; ENSGALP00000026013; ENSGALG00000016171. [Q00944-1]
GeneIDi396416.
KEGGigga:396416.

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86656 mRNA. Translation: AAA48765.1 .
L08402 mRNA. Translation: AAA48766.1 .
PIRi A45388.
PC1239.
RefSeqi NP_990766.1. NM_205435.1. [Q00944-1 ]
UniGenei Gga.15614.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KTM NMR - A 916-1053 [» ]
1PV3 NMR - A 920-1053 [» ]
1QVX NMR - A 920-1053 [» ]
2AEH X-ray 2.53 A/B 31-399 [» ]
2AL6 X-ray 2.35 A/B 31-405 [» ]
2J0J X-ray 2.80 A 31-686 [» ]
2J0K X-ray 3.00 A/B 31-686 [» ]
2J0L X-ray 2.30 A 411-686 [» ]
2J0M X-ray 2.80 A 31-399 [» ]
B 411-686 [» ]
2JKK X-ray 2.00 A 411-686 [» ]
2JKM X-ray 2.31 A 411-686 [» ]
2JKO X-ray 1.65 A 411-686 [» ]
2JKQ X-ray 2.60 A 411-686 [» ]
2L6F NMR - A 916-1053 [» ]
2L6G NMR - A 916-1053 [» ]
2L6H NMR - A 916-1053 [» ]
3ZDT X-ray 3.15 A/B 31-405 [» ]
4BRX X-ray 2.05 A 411-686 [» ]
4C7T X-ray 2.05 A 411-686 [» ]
4CYE X-ray 3.20 A/B 31-405 [» ]
ProteinModelPortali Q00944.
SMRi Q00944. Positions 33-686, 916-1053.
ModBasei Search...

Protein-protein interaction databases

BioGridi 676665. 2 interactions.
IntActi Q00944. 11 interactions.
MINTi MINT-1517788.

Proteomic databases

PaxDbi Q00944.
PRIDEi Q00944.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000026060 ; ENSGALP00000026013 ; ENSGALG00000016171 . [Q00944-1 ]
GeneIDi 396416.
KEGGi gga:396416.

Organism-specific databases

CTDi 5747.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000115459.
HOGENOMi HOG000069938.
HOVERGENi HBG004018.
KOi K05725.
PhylomeDBi Q00944.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1306.
Reactomei REACT_197606. Regulation of actin dynamics for phagocytic cup formation.
REACT_204997. Netrin mediated repulsion signals.
REACT_207020. DCC mediated attractive signaling.

Miscellaneous databases

EvolutionaryTracei Q00944.
NextBioi 20816457.
PROi Q00944.

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

  1. "pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions."
    Schaller M.D., Borgman C.A., Cobb B.S., Vines R.R., Reynolds A.B., Parsons J.T.
    Proc. Natl. Acad. Sci. U.S.A. 89:5192-5196(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-1053 (ISOFORM 1).
    Tissue: Embryo.
  2. "Chicken and mouse focal adhesion kinases are similar in structure at their amino termini."
    Devor B.B., Zhang X., Patel S.K., Polte T.R., Hanks S.K.
    Biochem. Biophys. Res. Commun. 190:1084-1089(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 1).
    Tissue: Embryo.
  3. "Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK."
    Schaller M.D., Borgman C.A., Parsons J.T.
    Mol. Cell. Biol. 13:785-791(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 2, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  4. "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase."
    Hildebrand J.D., Taylor J.M., Parsons J.T.
    Mol. Cell. Biol. 16:3169-3178(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP26.
  5. "Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration."
    Reiske H.R., Kao S.C., Cary L.A., Guan J.L., Lai J.F., Chen H.C.
    J. Biol. Chem. 274:12361-12366(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3R1 AND SRC, MUTAGENESIS OF ASP-395.
  6. "Association of Grb7 with phosphoinositides and its role in the regulation of cell migration."
    Shen T.L., Han D.C., Guan J.L.
    J. Biol. Chem. 277:29069-29077(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB7.
  7. "Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397."
    Leu T.H., Maa M.C.
    Oncogene 21:6992-7000(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.
  8. Cited for: FUNCTION, INTERACTION WITH DCC.
  9. "Activation of FAK and Src are receptor-proximal events required for netrin signaling."
    Li W., Lee J., Vikis H.G., Lee S.H., Liu G., Aurandt J., Shen T.L., Fearon E.R., Guan J.L., Han M., Rao Y., Hong K., Guan K.L.
    Nat. Neurosci. 7:1213-1221(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCC.
  10. "Netrin requires focal adhesion kinase and Src family kinases for axon outgrowth and attraction."
    Liu G., Beggs H., Jurgensen C., Park H.T., Tang H., Gorski J., Jones K.R., Reichardt L.F., Wu J., Rao Y.
    Nat. Neurosci. 7:1222-1232(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex."
    Serrels B., Serrels A., Brunton V.G., Holt M., McLean G.W., Gray C.H., Jones G.E., Frame M.C.
    Nat. Cell Biol. 9:1046-1056(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE ARP2/3 COMPLEX.
  12. "FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells."
    Koshman Y.E., Kim T., Chu M., Engman S.J., Iyengar R., Robia S.L., Samarel A.M.
    Arterioscler. Thromb. Vasc. Biol. 30:2226-2233(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Focal adhesion kinase-related nonkinase inhibits vascular smooth muscle cell invasion by focal adhesion targeting, tyrosine 168 phosphorylation, and competition for p130Cas Binding."
    Koshman Y.E., Chu M., Engman S.J., Kim T., Iyengar R., Robia S.L., Samarel A.M.
    Arterioscler. Thromb. Vasc. Biol. 31:2432-2440(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Serine-910 phosphorylation of focal adhesion kinase is critical for sarcomere reorganization in cardiomyocyte hypertrophy."
    Chu M., Iyengar R., Koshman Y.E., Kim T., Russell B., Martin J.L., Heroux A.L., Robia S.L., Samarel A.M.
    Cardiovasc. Res. 92:409-419(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-911, FUNCTION.
  15. "Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase."
    Liu G., Guibao C.D., Zheng J.
    Mol. Cell. Biol. 22:2751-2760(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 916-1053.
  16. "NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model."
    Gao G., Prutzman K.C., King M.L., Scheswohl D.M., DeRose E.F., London R.E., Schaller M.D., Campbell S.L.
    J. Biol. Chem. 279:8441-8451(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 920-1053 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
  17. "The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation."
    Prutzman K.C., Gao G., King M.L., Iyer V.V., Mueller G.A., Schaller M.D., Campbell S.L.
    Structure 12:881-891(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 920-1053.
  18. "Crystal structure of the FERM domain of focal adhesion kinase."
    Ceccarelli D.F., Song H.K., Poy F., Schaller M.D., Eck M.J.
    J. Biol. Chem. 281:252-259(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 31-405.
  19. "Structural basis for the autoinhibition of focal adhesion kinase."
    Lietha D., Cai X., Ceccarelli D.F., Li Y., Schaller M.D., Eck M.J.
    Cell 129:1177-1187(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 411-686 IN COMPLEXES WITH STAUROSPORINE AND ATP ANALOG, ENZYME REGULATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
  20. "Crystal structures of the FAK kinase in complex with TAE226 and related bis-anilino pyrimidine inhibitors reveal a helical DFG conformation."
    Lietha D., Eck M.J.
    PLoS ONE 3:E3800-E3800(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 411-686 IN COMPLEX WITH TAE226.

Entry informationi

Entry nameiFAK1_CHICK
AccessioniPrimary (citable) accession number: Q00944
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 138 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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