Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Focal adhesion kinase 1

Gene

PTK2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei454ATPCurated1
Active sitei546Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi428 – 434ATPCurated7
Nucleotide bindingi500 – 502ATPCurated3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent cysteine-type endopeptidase activity Source: AgBase
  • integrin binding Source: AgBase
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • protease binding Source: AgBase
  • protein tyrosine kinase activity Source: AgBase
  • signal transducer activity Source: InterPro

GO - Biological processi

  • actin filament organization Source: AgBase
  • angiogenesis involved in wound healing Source: AgBase
  • central nervous system neuron axonogenesis Source: Ensembl
  • endothelial cell migration Source: Ensembl
  • ephrin receptor signaling pathway Source: Ensembl
  • epidermal growth factor receptor signaling pathway Source: GO_Central
  • establishment of nucleus localization Source: Ensembl
  • extracellular matrix organization Source: Ensembl
  • growth hormone receptor signaling pathway Source: Ensembl
  • innate immune response Source: GO_Central
  • integrin-mediated signaling pathway Source: Ensembl
  • microtubule cytoskeleton organization Source: Ensembl
  • negative regulation of anoikis Source: AgBase
  • negative regulation of axonogenesis Source: Ensembl
  • negative regulation of cell-cell adhesion Source: Ensembl
  • negative regulation of cell-substrate adhesion Source: AgBase
  • negative regulation of organ growth Source: Ensembl
  • negative regulation of protein autophosphorylation Source: AgBase
  • negative regulation of synapse assembly Source: Ensembl
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • positive regulation of cell proliferation Source: AgBase
  • positive regulation of focal adhesion assembly Source: AgBase
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  • positive regulation of protein binding Source: AgBase
  • positive regulation of protein kinase B signaling Source: Ensembl
  • positive regulation of protein tyrosine kinase activity Source: AgBase
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  • positive regulation of substrate-dependent cell migration, cell attachment to substrate Source: AgBase
  • protein autophosphorylation Source: AgBase
  • pyramidal neuron migration Source: AgBase
  • regulation of cell adhesion mediated by integrin Source: Ensembl
  • regulation of cell shape Source: Ensembl
  • regulation of epithelial cell migration Source: Ensembl
  • regulation of osteoblast differentiation Source: Ensembl
  • regulation of substrate adhesion-dependent cell spreading Source: Ensembl
  • response to muscle stretch Source: AgBase
  • response to pH Source: AgBase
  • signal complex assembly Source: InterPro
  • transforming growth factor beta receptor signaling pathway Source: Ensembl
  • vasculogenesis Source: Ensembl
  • wound healing, spreading of cells Source: AgBase
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.
ReactomeiR-GGA-111465. Apoptotic cleavage of cellular proteins.
R-GGA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-GGA-354192. Integrin alphaIIb beta3 signaling.
R-GGA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-GGA-372708. p130Cas linkage to MAPK signaling for integrins.
R-GGA-375165. NCAM signaling for neurite out-growth.
R-GGA-3928662. EPHB-mediated forward signaling.
R-GGA-3928663. EPHA-mediated growth cone collapse.
R-GGA-418885. DCC mediated attractive signaling.
R-GGA-4420097. VEGFA-VEGFR2 Pathway.
R-GGA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-GGA-5673001. RAF/MAP kinase cascade.
R-GGA-8874081. MET activates PTK2 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • cell Source: AgBase
  • cytoplasm Source: AgBase
  • cytosol Source: Ensembl
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • focal adhesion Source: AgBase
  • lamellipodium Source: Ensembl
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • sarcolemma Source: AgBase
  • stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi395D → A: Abolishes interaction with PIK3R1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880761 – 1053Focal adhesion kinase 1Add BLAST1053

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei397Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei407PhosphotyrosineBy similarity1
Modified residuei576Phosphotyrosine; by SRC2 Publications1
Modified residuei577Phosphotyrosine; by SRCBy similarity1
Modified residuei863Phosphotyrosine1 Publication1
Modified residuei911Phosphoserine1 Publication1
Modified residuei926PhosphotyrosineBy similarity1

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.

PTM databases

iPTMnetiQ00944.

Expressioni

Gene expression databases

BgeeiENSGALG00000016171.
ExpressionAtlasiQ00944. baseline and differential.

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

GO - Molecular functioni

  • integrin binding Source: AgBase
  • protease binding Source: AgBase

Protein-protein interaction databases

BioGridi676665. 2 interactors.
IntActiQ00944. 11 interactors.
MINTiMINT-1517788.
STRINGi9031.ENSGALP00000026014.

Structurei

Secondary structure

11053
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 40Combined sources5
Helixi49 – 51Combined sources3
Beta strandi53 – 58Combined sources6
Helixi64 – 74Combined sources11
Helixi80 – 82Combined sources3
Beta strandi83 – 89Combined sources7
Beta strandi95 – 98Combined sources4
Beta strandi100 – 103Combined sources4
Helixi104 – 112Combined sources9
Helixi117 – 119Combined sources3
Beta strandi120 – 126Combined sources7
Helixi133 – 137Combined sources5
Helixi141 – 158Combined sources18
Turni159 – 162Combined sources4
Helixi165 – 179Combined sources15
Turni180 – 182Combined sources3
Helixi187 – 189Combined sources3
Helixi191 – 199Combined sources9
Turni200 – 202Combined sources3
Helixi203 – 205Combined sources3
Helixi209 – 213Combined sources5
Helixi217 – 229Combined sources13
Turni230 – 233Combined sources4
Helixi236 – 247Combined sources12
Turni248 – 250Combined sources3
Beta strandi256 – 262Combined sources7
Beta strandi264 – 266Combined sources3
Beta strandi268 – 275Combined sources8
Turni276 – 278Combined sources3
Beta strandi279 – 285Combined sources7
Beta strandi290 – 294Combined sources5
Helixi296 – 298Combined sources3
Beta strandi299 – 305Combined sources7
Beta strandi308 – 310Combined sources3
Beta strandi314 – 320Combined sources7
Beta strandi327 – 333Combined sources7
Helixi334 – 352Combined sources19
Beta strandi398 – 402Combined sources5
Helixi412 – 414Combined sources3
Helixi419 – 421Combined sources3
Beta strandi422 – 431Combined sources10
Beta strandi434 – 441Combined sources8
Beta strandi444 – 446Combined sources3
Beta strandi449 – 455Combined sources7
Turni457 – 460Combined sources4
Helixi462 – 475Combined sources14
Beta strandi486 – 490Combined sources5
Beta strandi492 – 494Combined sources3
Beta strandi496 – 500Combined sources5
Helixi507 – 514Combined sources8
Turni515 – 517Combined sources3
Helixi520 – 539Combined sources20
Helixi549 – 551Combined sources3
Beta strandi552 – 556Combined sources5
Beta strandi559 – 562Combined sources4
Helixi567 – 570Combined sources4
Helixi572 – 575Combined sources4
Helixi577 – 579Combined sources3
Helixi586 – 588Combined sources3
Helixi591 – 596Combined sources6
Helixi601 – 616Combined sources16
Turni617 – 619Combined sources3
Turni622 – 625Combined sources4
Helixi628 – 630Combined sources3
Helixi631 – 636Combined sources6
Helixi649 – 658Combined sources10
Helixi663 – 665Combined sources3
Helixi669 – 684Combined sources16
Turni919 – 921Combined sources3
Helixi922 – 941Combined sources20
Turni942 – 945Combined sources4
Helixi948 – 975Combined sources28
Turni978 – 980Combined sources3
Helixi982 – 1005Combined sources24
Beta strandi1008 – 1012Combined sources5
Helixi1014 – 1047Combined sources34

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4D4RX-ray1.55A/B411-686[»]
4D4SX-ray2.00A/B411-686[»]
4D4VX-ray2.10A/B411-686[»]
4D4YX-ray1.80A/B411-686[»]
4D55X-ray2.30A411-686[»]
4D58X-ray1.95A/B411-686[»]
4D5HX-ray1.75A/B411-686[»]
4D5KX-ray1.75A/B411-686[»]
ProteinModelPortaliQ00944.
SMRiQ00944.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00944.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 355FERMPROSITE-ProRule annotationAdd BLAST321
Domaini422 – 680Protein kinasePROSITE-ProRule annotationAdd BLAST259

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi712 – 733Pro-richAdd BLAST22
Compositional biasi865 – 914Pro-richAdd BLAST50

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

eggNOGiKOG4257. Eukaryota.
ENOG410ZH9Y. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000069938.
HOVERGENiHBG004018.
InParanoidiQ00944.
KOiK05725.
OMAiKSGCSPF.
OrthoDBiEOG091G03BN.
PhylomeDBiQ00944.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
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.
SSF50729. SSF50729. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0421731 – 692Missing in isoform 2. CuratedAdd BLAST692

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

EnsembliENSGALT00000072414; ENSGALP00000044406; ENSGALG00000031741. [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.
PIRiA45388.
PC1239.
RefSeqiNP_990766.1. NM_205435.1. [Q00944-1]
UniGeneiGga.15614.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4D4RX-ray1.55A/B411-686[»]
4D4SX-ray2.00A/B411-686[»]
4D4VX-ray2.10A/B411-686[»]
4D4YX-ray1.80A/B411-686[»]
4D55X-ray2.30A411-686[»]
4D58X-ray1.95A/B411-686[»]
4D5HX-ray1.75A/B411-686[»]
4D5KX-ray1.75A/B411-686[»]
ProteinModelPortaliQ00944.
SMRiQ00944.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676665. 2 interactors.
IntActiQ00944. 11 interactors.
MINTiMINT-1517788.
STRINGi9031.ENSGALP00000026014.

PTM databases

iPTMnetiQ00944.

Proteomic databases

PaxDbiQ00944.
PRIDEiQ00944.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000072414; ENSGALP00000044406; ENSGALG00000031741. [Q00944-1]
GeneIDi396416.
KEGGigga:396416.

Organism-specific databases

CTDi5747.

Phylogenomic databases

eggNOGiKOG4257. Eukaryota.
ENOG410ZH9Y. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000069938.
HOVERGENiHBG004018.
InParanoidiQ00944.
KOiK05725.
OMAiKSGCSPF.
OrthoDBiEOG091G03BN.
PhylomeDBiQ00944.

Enzyme and pathway databases

BRENDAi2.7.10.2. 1306.
ReactomeiR-GGA-111465. Apoptotic cleavage of cellular proteins.
R-GGA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-GGA-354192. Integrin alphaIIb beta3 signaling.
R-GGA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-GGA-372708. p130Cas linkage to MAPK signaling for integrins.
R-GGA-375165. NCAM signaling for neurite out-growth.
R-GGA-3928662. EPHB-mediated forward signaling.
R-GGA-3928663. EPHA-mediated growth cone collapse.
R-GGA-418885. DCC mediated attractive signaling.
R-GGA-4420097. VEGFA-VEGFR2 Pathway.
R-GGA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-GGA-5673001. RAF/MAP kinase cascade.
R-GGA-8874081. MET activates PTK2 signaling.

Miscellaneous databases

EvolutionaryTraceiQ00944.
PROiQ00944.

Gene expression databases

BgeeiENSGALG00000016171.
ExpressionAtlasiQ00944. baseline and differential.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
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.
SSF50729. SSF50729. 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]
ProtoNetiSearch...

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 30, 2016
This is version 162 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.