dbPTM

FAK1_CHICK - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAK1_CHICK
UniProt AC	Q00944
Protein Name	Focal adhesion kinase 1
Gene Name	PTK2
Organism	Gallus gallus (Chicken).
Sequence Length	1053
Subcellular Localization	Cell junction, focal adhesion . Cell membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm, perinuclear region . Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus . Constituent of foc
Protein Description	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..
Protein Sequence	MAAAYLDPNLNHTPSSSAKTHLGTGMERSPGAMERVLKVFHYFENSSEPTTWASIIRHGDATDVRGIIQKIVDCHKVKNVACYGLRLSHLQSEEVHWLHLDMGVSNVREKFELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKNDYMLEIADQVDQEIALKLGCLEIRRSYGEMRGNALEKKSNYEVLEKDVGLRRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGANPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGVRSHTVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAMAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKLQQEERMRMESRRQVTVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQPNHYQVSGYSGSHGIPAMAGSIYPGQASLLDQTDSWNHRPQEVSAWQPNMEDSGTLDVRGMGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLVMKPDVRLSRGSIEREDGGLQGPAGNQHIYQPVGKPDHAAPPKKPPRPGAPHLGSLASLNSPVDSYNEGVKIKPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDESLPVLPASTHREIEMAQKLLNSDLAELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMISQSRPH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	LDPNLNHTPSSSAKT CCCCCCCCCCCCCCC	24.64	16254240
29	Phosphorylation	LGTGMERSPGAMERV CCCCCCCCCCHHHHH	17.87	16254240
155	Phosphorylation	YQQVKNDYMLEIADQ HHHHCCCHHHHHHHH	17.00	16254240
386	Phosphorylation	NEKQGVRSHTVSVSE CCCCCCCCEECEEEC	22.54	16254240
388	Phosphorylation	KQGVRSHTVSVSETD CCCCCCEECEEECCC	18.74	16254240
390	Phosphorylation	GVRSHTVSVSETDDY CCCCEECEEECCCCC	22.53	16254240
392	Phosphorylation	RSHTVSVSETDDYAE CCEECEEECCCCCCE	27.54	16254240
397	Phosphorylation	SVSETDDYAEIIDEE EEECCCCCCEECCCC	14.67	12370821
406	Phosphorylation	EIIDEEDTYTMPSTR EECCCCCCCCCCCCC	24.95	16254240
407	Phosphorylation	IIDEEDTYTMPSTRD ECCCCCCCCCCCCCC	17.23	16254240
570	Phosphorylation	GDFGLSRYMEDSTYY CCCCHHHHHCCCCEE	11.07	16254240
576	Phosphorylation	RYMEDSTYYKASKGK HHHCCCCEECCCCCC	13.61	12370821
577	Phosphorylation	YMEDSTYYKASKGKL HHCCCCEECCCCCCC	10.52	-
700	Phosphorylation	MESRRQVTVSWDSGG HHHHCCCEEEECCCC	10.65	16254240
708	Phosphorylation	VSWDSGGSDEAPPKP EEECCCCCCCCCCCC	35.48	16254240
722	Phosphorylation	PSRPGYPSPRSSEGF CCCCCCCCCCCCCCC	25.18	16254240
726	Phosphorylation	GYPSPRSSEGFYPSP CCCCCCCCCCCCCCC	42.91	-
732	Phosphorylation	SSEGFYPSPQHMVQP CCCCCCCCCCCCCCC	26.30	16254240
766	Phosphorylation	SIYPGQASLLDQTDS CCCCCCCHHHCCCCC	22.90	16254240
793	Phosphorylation	PNMEDSGTLDVRGMG CCCCCCCCCCCCCCC	24.60	16254240
842	Phosphorylation	MKPDVRLSRGSIERE ECCCCEECCCCEECC	24.83	-
845	Phosphorylation	DVRLSRGSIEREDGG CCEECCCCEECCCCC	21.84	16254240
863	Phosphorylation	PAGNQHIYQPVGKPD CCCCCEEECCCCCCC	12.49	12370821
888	Phosphorylation	PGAPHLGSLASLNSP CCCCCCCCHHHCCCC	27.42	16254240
891	Phosphorylation	PHLGSLASLNSPVDS CCCCCHHHCCCCCCC	33.12	16254240
894	Phosphorylation	GSLASLNSPVDSYNE CCHHHCCCCCCCCCC	31.43	16254240
898	Phosphorylation	SLNSPVDSYNEGVKI HCCCCCCCCCCCCCC	30.05	16254240
899	Phosphorylation	LNSPVDSYNEGVKIK CCCCCCCCCCCCCCC	16.87	16254240
911	Phosphorylation	KIKPQEISPPPTANL CCCCCCCCCCCCCCC	30.51	21736374
926	Phosphorylation	DRSNDKVYENVTGLV CCCCCHHHHCHHHHH	13.92	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
397	Y	Phosphorylation	Kinase	PTK2	Q00944	GPS
576	Y	Phosphorylation	Kinase	SRC	P00523	Uniprot
577	Y	Phosphorylation	Kinase	SRC	P00523	Uniprot
722	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
926	Y	Phosphorylation	Kinase	SRC	P00523	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FAK1_CHICK !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of FAK1_CHICK !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of FAK1_CHICK !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FAK1_CHICK

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Serine-910 phosphorylation of focal adhesion kinase is critical forsarcomere 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). Cited for: PHOSPHORYLATION AT SER-911, AND FUNCTION.	21937583 [Abstract]
"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). Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 411-686 IN COMPLEXES WITHSTAUROSPORINE AND ATP ANALOG, ENZYME REGULATION, AND PHOSPHORYLATIONAT TYR-576 AND TYR-577.	17574028 [Abstract]
"Tyr-863 phosphorylation enhances focal adhesion kinaseautophosphorylation at Tyr-397."; Leu T.H., Maa M.C.; Oncogene 21:6992-7000(2002). Cited for: PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.	12370821 [Abstract]