logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0122 : Focal adhesion kinase, FAK

[ CaMP Format ]

* Basic Information

OrganismMus musculus (house mouse)
Protein Namesfocal adhesion kinase 1 isoform 1 [Mus musculus]; focal adhesion kinase 1 isoform 1; focal adhesion kinase 1; FADK 1; pp125FAK; protein-tyrosine kinase 2; focal adhesion kinase-related nonkinase; focal ashension kinase 1
Gene NamesPtk2; PTK2 protein tyrosine kinase 2
Gene Locus15 33.94 cM; chromosome 15
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_032008 NM_007982 14083 N/A N/A N/A N/A N/A

* Information From OMIM

Not Available.

* Structure Information

1. Primary Information

Length: 1052 aa

Average Mass: 119.242 kDa

Monoisotopic Mass: 119.167 kDa

2. Domain Information

Annotated Domains: Not Available.

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
FERM central domain 1. 1382515.00.2
FERM central domain 2. 45147880.00.0
Kinase-like 1. 501615125.00.0
--- cleavage 745 ---
FERM central domain 3. 986101858.00.0

3. Sequence Information

Fasta Sequence: SB0122.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Not Available.

* Cleavage Information

1 [sites] cleaved by Calpain 2

Source Reference: [PubMed ID: 20150423] Chan KT, Bennin DA, Huttenlocher A, Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK). J Biol Chem. 2010 Apr 9;285(15):11418-26. doi: 10.1074/jbc.M109.090746. Epub 2010

Cleavage sites (±10aa)

[Site 1] MVQTNHYQVS745-GYPGSHGIPA

Ser745 Gly

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Met736Val737Gln738Thr739Asn740His741Tyr742Gln743Val744Ser745
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Gly746Tyr747Pro748Gly749Ser750His751Gly752Ile753Pro754Ala755

Sequence conservation (by blast)

* References

[PubMed ID: 24344130] Nguyen N, Yi JS, Park H, Lee JS, Ko YG, Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis. J Biol Chem. 2014 Feb 7;289(6):3209-16. doi: 10.1074/jbc.M113.525154. Epub 2013

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