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Q00944

- FAK1_CHICK

UniProt

Q00944 - FAK1_CHICK

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Protein

Focal adhesion kinase 1

Gene

PTK2

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.PROSITE-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 TAE226.1 Publication

Sites

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

Regions

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

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. signal transducer activity Source: InterPro

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.
REACT_235751. EPHB-mediated forward signaling.
REACT_238229. Apoptotic cleavage of cellular proteins.
REACT_240643. p130Cas linkage to MAPK signaling for integrins.
REACT_246525. NCAM signaling for neurite out-growth.
REACT_250039. VEGFA-VEGFR2 Pathway.
REACT_253932. EPHA-mediated growth cone collapse.
REACT_257604. Integrin alphaIIb beta3 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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 2

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. focal adhesion Source: InterPro
  4. nucleus Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB-KW
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 1PRO_0000088076Add
BLAST

Amino acid modifications

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

Expressioni

Gene expression databases

ExpressionAtlasiQ00944. baseline.

Interactioni

Subunit structurei

Interacts with ARHGAP26, GRB7, DCC, PIK3R1, PXN and SRC. Interacts with the ARP2/3 complex.8 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

1
1053
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 405Combined sources
Helixi49 – 513Combined sources
Beta strandi53 – 586Combined sources
Helixi64 – 7411Combined sources
Helixi80 – 823Combined sources
Beta strandi83 – 897Combined sources
Beta strandi95 – 984Combined sources
Beta strandi100 – 1034Combined sources
Helixi104 – 1129Combined sources
Helixi117 – 1193Combined sources
Beta strandi120 – 1267Combined sources
Helixi133 – 1375Combined sources
Helixi141 – 15818Combined sources
Turni159 – 1624Combined sources
Helixi165 – 17915Combined sources
Turni180 – 1823Combined sources
Helixi187 – 1893Combined sources
Helixi191 – 1999Combined sources
Turni200 – 2023Combined sources
Helixi203 – 2053Combined sources
Helixi209 – 2135Combined sources
Helixi217 – 22913Combined sources
Turni230 – 2334Combined sources
Helixi236 – 24712Combined sources
Turni248 – 2503Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi268 – 2758Combined sources
Turni276 – 2783Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi290 – 2945Combined sources
Helixi296 – 2983Combined sources
Beta strandi299 – 3057Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi314 – 3207Combined sources
Beta strandi327 – 3337Combined sources
Helixi334 – 35219Combined sources
Beta strandi398 – 4025Combined sources
Helixi412 – 4143Combined sources
Helixi419 – 4213Combined sources
Beta strandi422 – 4309Combined sources
Beta strandi432 – 44110Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi448 – 4558Combined sources
Turni457 – 4604Combined sources
Helixi462 – 47615Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi492 – 4943Combined sources
Beta strandi496 – 5005Combined sources
Helixi507 – 5137Combined sources
Turni514 – 5174Combined sources
Helixi520 – 53920Combined sources
Helixi549 – 5513Combined sources
Beta strandi552 – 5565Combined sources
Beta strandi559 – 5624Combined sources
Helixi565 – 5684Combined sources
Beta strandi573 – 5753Combined sources
Helixi586 – 5883Combined sources
Helixi591 – 5966Combined sources
Helixi601 – 61616Combined sources
Turni617 – 6193Combined sources
Turni622 – 6254Combined sources
Helixi628 – 6303Combined sources
Helixi631 – 6366Combined sources
Helixi649 – 65810Combined sources
Helixi663 – 6653Combined sources
Helixi669 – 68517Combined sources
Turni919 – 9213Combined sources
Helixi922 – 94120Combined sources
Turni942 – 9454Combined sources
Helixi948 – 97528Combined sources
Turni978 – 9803Combined sources
Helixi982 – 100524Combined sources
Beta strandi1008 – 10125Combined sources
Helixi1014 – 104734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00944.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

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.
InParanoidiQ00944.
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

        10         20         30         40         50
MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT
60 70 80 90 100
TWASIIRHGD ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL
110 120 130 140 150
DMGVSNVREK FELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190 200
VKNDYMLEIA DQVDQEIALK LGCLEIRRSY GEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGATQSFII RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPAMA
460 470 480 490 500
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME
510 520 530 540 550
LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590 600
NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
610 620 630 640 650
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT
660 670 680 690 700
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS
760 770 780 790 800
HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE VSAWQPNMED SGTLDVRGMG
810 820 830 840 850
QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR LSRGSIERED
860 870 880 890 900
GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN
910 920 930 940 950
EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE
960 970 980 990 1000
YVPMVKEVGL ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN
1010 1020 1030 1040 1050
KMKLAQQYVM TSLQQEYKKQ MLTAAHALAV DAKNLLDVID QARLKMISQS

RPH
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. CuratedVSP_042173Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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 ENSGT00760000118799.
HOGENOMi HOG000069938.
HOVERGENi HBG004018.
InParanoidi Q00944.
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.
REACT_235751. EPHB-mediated forward signaling.
REACT_238229. Apoptotic cleavage of cellular proteins.
REACT_240643. p130Cas linkage to MAPK signaling for integrins.
REACT_246525. NCAM signaling for neurite out-growth.
REACT_250039. VEGFA-VEGFR2 Pathway.
REACT_253932. EPHA-mediated growth cone collapse.
REACT_257604. Integrin alphaIIb beta3 signaling.

Miscellaneous databases

EvolutionaryTracei Q00944.
NextBioi 20816457.
PROi Q00944.

Gene expression databases

ExpressionAtlasi Q00944. baseline.

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: November 26, 2014
This is version 141 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