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Reviewed, UniProtKB/Swiss-Prot Q00944 (FAK1_CHICK)

Last modified October 13, 2009. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Focal adhesion kinase 1
      Short name=FADK 1
    EC=2.7.10.2
Alternative name(s):
    pp125FAK
Gene names
Name: FAK1
Synonyms: FAK
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length1053 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity.

Catalytic activity

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

Subcellular location

Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Constituent of focal adhesions.

Domain

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

Post-translational modification

Phosphorylated on 6 tyrosine residues upon activation. Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.

Contains 1 FERM domain.

Contains 1 protein kinase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10531053Focal adhesion kinase 1
PRO_0000088076

Regions

Domain35 – 355321FERM
Domain422 – 680259Protein kinase
Nucleotide binding428 – 4369ATP By similarity
Compositional bias712 – 73322Pro-rich
Compositional bias865 – 91450Pro-rich

Sites

Active site5461Proton acceptor By similarity
Binding site4541ATP By similarity

Amino acid modifications

Modified residue3971Phosphotyrosine Ref.3
Modified residue4071Phosphotyrosine By similarity
Modified residue5761Phosphotyrosine; by autocatalysis Ref.3
Modified residue5771Phosphotyrosine; by autocatalysis By similarity
Modified residue8631Phosphotyrosine Ref.3
Modified residue9261Phosphotyrosine By similarity

Secondary structure

1 .......................................................................................................................... 1053
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q00944-1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 8051154219B953B9

FASTA1,053119,207
        10         20         30         40         50         60 
MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT TWASIIRHGD 

        70         80         90        100        110        120 
ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL DMGVSNVREK FELAHPPEEW 

       130        140        150        160        170        180 
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKNDYMLEIA DQVDQEIALK LGCLEIRRSY 

       190        200        210        220        230        240 
GEMRGNALEK KSNYEVLEKD VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 

       250        260        270        280        290        300 
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ 

       310        320        330        340        350        360 
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 

       370        380        390        400        410        420 
RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 

       430        440        450        460        470        480 
RIELGRCIGE GQFGDVHQGI YMSPENPAMA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 

       490        500        510        520        530        540 
PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK 

       550        560        570        580        590        600 
RFVHRDIAAR NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 

       610        620        630        640        650        660 
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 

       670        680        690        700        710        720 
YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT VSWDSGGSDE APPKPSRPGY 

       730        740        750        760        770        780 
PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE 

       790        800        810        820        830        840 
VSAWQPNMED SGTLDVRGMG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR 

       850        860        870        880        890        900 
LSRGSIERED GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN 

       910        920        930        940        950        960 
EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL 

       970        980        990       1000       1010       1020 
ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN KMKLAQQYVM TSLQQEYKKQ 

      1030       1040       1050 
MLTAAHALAV DAKNLLDVID QARLKMISQS RPH

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References

[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: 1594631] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-1053.
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: 8439308] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63.
Tissue: Embryo.
[3]"Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397."
Leu T.H., Maa M.C.
Oncogene 21:6992-7000(2002) [PubMed: 12370821] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M86656 mRNA. Translation: AAA48765.1.
L08402 mRNA. Translation: AAA48766.1.
IPIIPI00591393.
PIRA45388.
PC1239.
RefSeqNP_990766.1.
UniGeneGga.42870

3D structure databases

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[»]
SMRQ00944. Positions 909-1050.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ00944.

Proteomic databases

PRIDEQ00944.

Genome annotation databases

EnsemblENSGALT00000026060; ENSGALP00000026013; ENSGALG00000016171; Gallus gallus. [Genome view]
ENSGALT00000026061; ENSGALP00000026014; ENSGALG00000016171; Gallus gallus. [Genome view]
GeneID396416.
KEGGgga:396416.

Organism-specific databases

CTD396416.

Phylogenomic databases

HOVERGENQ00944.

Enzyme and pathway databases

BRENDA2.7.10.2. 4.

Family and domain databases

InterProIPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_target_reg.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00660. FERM_1. False negative.
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]
ProtoNetSearch...

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Entry information

Entry nameFAK1_CHICK
AccessionPrimary (citable) accession number: Q00944
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1994
Last modified: October 13, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents