dbPTM

FAK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAK1_HUMAN
UniProt AC	Q05397
Protein Name	Focal adhesion kinase 1
Gene Name	PTK2
Organism	Homo sapiens (Human).
Sequence Length	1052
Subcellular Localization	Cell junction, focal adhesion. Cell membrane Peripheral membrane protein Cytoplasmic side. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Constituent of focal adhesions.
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 and placenta development. Required for 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), EPHA2, 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. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription..
Protein Sequence	MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAYLDPN ------CCCCCCCCC	16.47	19369195
5	Phosphorylation	---MAAAYLDPNLNH ---CCCCCCCCCCCC	13.60	25159151
13	Phosphorylation	LDPNLNHTPNSSTKT CCCCCCCCCCCCCCC	24.08	25159151
16	Phosphorylation	NLNHTPNSSTKTHLG CCCCCCCCCCCCCCC	40.36	25159151
17	Phosphorylation	LNHTPNSSTKTHLGT CCCCCCCCCCCCCCC	40.33	22199227
18	Phosphorylation	NHTPNSSTKTHLGTG CCCCCCCCCCCCCCC	39.52	22199227
20	Phosphorylation	TPNSSTKTHLGTGME CCCCCCCCCCCCCCC	23.56	23403867
24	Phosphorylation	STKTHLGTGMERSPG CCCCCCCCCCCCCCC	39.45	27696853
29	Phosphorylation	LGTGMERSPGAMERV CCCCCCCCCCHHHHH	17.87	25159151
54	Phosphorylation	SEPTTWASIIRHGDA CCCCCHHHHHHCCCC	15.31	-
65	Methylation	HGDATDVRGIIQKIV CCCCCCHHHHHHHHH	33.14	-
70	Ubiquitination	DVRGIIQKIVDSHKV CHHHHHHHHHHCCCC	34.00	-
131	Sumoylation	LRIRYLPKGFLNQFT EEEEECCCCHHHHHC	60.75	-
131	Sumoylation	LRIRYLPKGFLNQFT EEEEECCCCHHHHHC	60.75	14500712
148	Phosphorylation	KPTLNFFYQQVKSDY CCCHHHHHHHHCCCH	8.22	17117420
152	Sumoylation	NFFYQQVKSDYMLEI HHHHHHHCCCHHHHH	33.02	-
155	Phosphorylation	YQQVKSDYMLEIADQ HHHHCCCHHHHHHHH	15.64	17117420
194	Phosphorylation	ALEKKSNYEVLEKDV HHHHHCCHHHHHHHH	17.95	20802513
199	Ubiquitination	SNYEVLEKDVGLKRF CCHHHHHHHHCCHHH	54.26	-
216	Ubiquitination	KSLLDSVKAKTLRKL HHHHHHHHHHHHHHH	48.38	-
222	Malonylation	VKAKTLRKLIQQTFR HHHHHHHHHHHHHHH	53.72	26320211
239	Phosphorylation	ANLNREESILKFFEI HCCCHHHHHHHHHHH	28.59	24719451
248	Phosphorylation	LKFFEILSPVYRFDK HHHHHHHCCHHCCCH	20.27	21406692
251	Phosphorylation	FEILSPVYRFDKECF HHHHCCHHCCCHHHH	14.67	21406692
347	Phosphorylation	MADLIDGYCRLVNGT HHHHHHHCHHHHCCC	3.17	11853674
364	Ubiquitination	SFIIRPQKEGERALP CEEECCCCCCCCCCC	71.07	-
372	Phosphorylation	EGERALPSIPKLANS CCCCCCCCCHHHCCC	52.99	23532336
386	Phosphorylation	SEKQGMRTHAVSVSE CCCCCCCCEEEEECC	12.80	28176443
390	Phosphorylation	GMRTHAVSVSETDDY CCCCEEEEECCCCCC	22.25	22322096
392	Phosphorylation	RTHAVSVSETDDYAE CCEEEEECCCCCCHH	27.54	28176443
394	Phosphorylation	HAVSVSETDDYAEII EEEEECCCCCCHHCC	27.02	28176443
397	Dephosphorylation	SVSETDDYAEIIDEE EECCCCCCHHCCCCC	14.67	11314030
397	Phosphorylation	SVSETDDYAEIIDEE EECCCCCCHHCCCCC	14.67	12754219
406	Phosphorylation	EIIDEEDTYTMPSTR HCCCCCCCCCCCCCC	24.95	28176443
407	Phosphorylation	IIDEEDTYTMPSTRD CCCCCCCCCCCCCCC	17.23	17449913
408	Phosphorylation	IDEEDTYTMPSTRDY CCCCCCCCCCCCCCH	25.38	18691976
411	Phosphorylation	EDTYTMPSTRDYEIQ CCCCCCCCCCCHHHH	25.83	26356563
412	Phosphorylation	DTYTMPSTRDYEIQR CCCCCCCCCCHHHHH	22.99	26356563
441	Phosphorylation	GDVHQGIYMSPENPA CCCCCCEEECCCCHH	9.81	27259358
443	Phosphorylation	VHQGIYMSPENPALA CCCCEEECCCCHHHH	16.46	26356563
460	Phosphorylation	IKTCKNCTSDSVREK HHHCCCCCCHHHHHH	44.99	-
461	Phosphorylation	KTCKNCTSDSVREKF HHCCCCCCHHHHHHH	30.04	-
463	Phosphorylation	CKNCTSDSVREKFLQ CCCCCCHHHHHHHHH	23.88	-
467	Acetylation	TSDSVREKFLQEALT CCHHHHHHHHHHHHH	40.59	19828921
474	Phosphorylation	KFLQEALTMRQFDHP HHHHHHHHHHHCCCC	19.84	-
503	Phosphorylation	WIIMELCTLGELRSF HHHHHHCCHHHHHHH	50.88	17117420
517	Phosphorylation	FLQVRKYSLDLASLI HHHHHHHHHHHHHHH	20.60	20860994
522	Phosphorylation	KYSLDLASLILYAYQ HHHHHHHHHHHHHHH	24.20	20860994
526	Phosphorylation	DLASLILYAYQLSTA HHHHHHHHHHHHHHH	9.03	20860994
568	Phosphorylation	KLGDFGLSRYMEDST EECCCCHHHHHCCCC	23.03	29255136
570	Phosphorylation	GDFGLSRYMEDSTYY CCCCHHHHHCCCCEE	11.07	21945579
574	Phosphorylation	LSRYMEDSTYYKASK HHHHHCCCCEECCCC	12.66	21945579
575	Phosphorylation	SRYMEDSTYYKASKG HHHHCCCCEECCCCC	43.10	21945579
576	Phosphorylation	RYMEDSTYYKASKGK HHHCCCCEECCCCCC	13.61	19664994
577	Phosphorylation	YMEDSTYYKASKGKL HHCCCCEECCCCCCC	10.52	17449913
580	Phosphorylation	DSTYYKASKGKLPIK CCCEECCCCCCCCCE	37.48	27273156
677	Phosphorylation	TELKAQLSTILEEEK HHHHHHHHHHHHHHH	11.00	30624053
678	Phosphorylation	ELKAQLSTILEEEKA HHHHHHHHHHHHHHH	37.87	30624053
684	Ubiquitination	STILEEEKAQQEERM HHHHHHHHHHHHHHH	55.57	-
688 (in isoform 2)	Phosphorylation	-	35.17	28796482
695	Phosphorylation	EERMRMESRRQATVS HHHHHHHHHHHCEEC	24.34	-
700	Phosphorylation	MESRRQATVSWDSGG HHHHHHCEECCCCCC	13.51	23663014
702	Phosphorylation	SRRQATVSWDSGGSD HHHHCEECCCCCCCC	22.32	23927012
705	Phosphorylation	QATVSWDSGGSDEAP HCEECCCCCCCCCCC	38.50	23927012
708	Phosphorylation	VSWDSGGSDEAPPKP ECCCCCCCCCCCCCC	35.48	23927012
716	Phosphorylation	DEAPPKPSRPGYPSP CCCCCCCCCCCCCCC	58.18	30266825
720	Phosphorylation	PKPSRPGYPSPRSSE CCCCCCCCCCCCCCC	11.83	23927012
722	Phosphorylation	PSRPGYPSPRSSEGF CCCCCCCCCCCCCCC	25.18	19664994
725 (in isoform 7)	Phosphorylation	-	35.80	22210691
726	Phosphorylation	GYPSPRSSEGFYPSP CCCCCCCCCCCCCCC	42.91	-
726 (in isoform 7)	Phosphorylation	-	42.91	22210691
732	Phosphorylation	SSEGFYPSPQHMVQT CCCCCCCCCCCEEEE	26.30	17096371
742	Phosphorylation	HMVQTNHYQVSGYPG CEEEECCEECCCCCC	16.81	-
759	Phosphorylation	GITAMAGSIYPGQAS CEEEEECCCCCCCHH	14.92	-
759 (in isoform 7)	Phosphorylation	-	14.92	22210691
761	Phosphorylation	TAMAGSIYPGQASLL EEEECCCCCCCHHHH	11.74	-
805	Phosphorylation	GIGQVLPTHLMEERL CCCHHHCHHHHHHHH	24.39	17855441
840	Phosphorylation	LKPDVRLSRGSIDRE CCCCCEECCCCCCCC	24.83	28355574
843	Phosphorylation	DVRLSRGSIDREDGS CCEECCCCCCCCCCC	21.87	21945579
850	Phosphorylation	SIDREDGSLQGPIGN CCCCCCCCEECCCCC	29.82	21945579
861	Phosphorylation	PIGNQHIYQPVGKPD CCCCEEEECCCCCCC	12.49	17449913
861 (in isoform 5)	Phosphorylation	-	12.49	-
887	Phosphorylation	GAPGHLGSLASLSSP CCCCCHHHHHHCCCC	27.42	21082442
890	Phosphorylation	GHLGSLASLSSPADS CCHHHHHHCCCCCCC	33.79	26356563
892	Phosphorylation	LGSLASLSSPADSYN HHHHHHCCCCCCCCC	31.61	26356563
893	Phosphorylation	GSLASLSSPADSYNE HHHHHCCCCCCCCCC	29.42	29496963
897	Phosphorylation	SLSSPADSYNEGVKL HCCCCCCCCCCCCCC	31.78	23186163
898	Phosphorylation	LSSPADSYNEGVKLQ CCCCCCCCCCCCCCC	20.13	25884760
910	Phosphorylation	KLQPQEISPPPTANL CCCCCCCCCCCCCCC	30.51	17096371
914	Phosphorylation	QEISPPPTANLDRSN CCCCCCCCCCCCCCC	33.67	23927012
920	Phosphorylation	PTANLDRSNDKVYEN CCCCCCCCCCHHHHC	49.39	28152594
923	Ubiquitination	NLDRSNDKVYENVTG CCCCCCCHHHHCHHH	51.47	-
923 (in isoform 5)	Phosphorylation	-	51.47	30087585
925	Phosphorylation	DRSNDKVYENVTGLV CCCCCHHHHCHHHHH	13.92	12754219
929	Phosphorylation	DKVYENVTGLVKAVI CHHHHCHHHHHHHHH	36.06	28152594
963	Phosphorylation	EVGLALRTLLATVDE HHHHHHHHHHHHHCC	27.29	-
967	Phosphorylation	ALRTLLATVDETIPL HHHHHHHHHCCCCCC	28.58	-
971	Phosphorylation	LLATVDETIPLLPAS HHHHHCCCCCCCCCC	24.35	-
1000	Ubiquitination	DLGELINKMKLAQQY CHHHHHHHHHHHHHH	30.34	-
1007	Phosphorylation	KMKLAQQYVMTSLQQ HHHHHHHHHHHHHHH	4.70	17117420
1016	Phosphorylation	MTSLQQEYKKQMLTA HHHHHHHHHHHHHHH	21.10	18083107
1017	Acetylation	TSLQQEYKKQMLTAA HHHHHHHHHHHHHHH	35.46	24179899

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
5	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
5	Y	Phosphorylation	Kinase	MET	P08581	PSP
5	Y	Phosphorylation	Kinase	PDGFRB	P09619	PSP
194	Y	Phosphorylation	Kinase	MET	P08581	PSP
194	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
194	Y	Phosphorylation	Kinase	PDGFRB	P09619	PSP
194	Y	Phosphorylation	Kinase	BMX	P51813	GPS
194	Y	Phosphorylation	Kinase	SRC	P12931	PSP
397	Y	Phosphorylation	Kinase	MET	P08581	PSP
397	Y	Phosphorylation	Kinase	SRC	P12931	PSP
397	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
397	Y	Phosphorylation	Kinase	FGR	P09769	PSP
407	Y	Phosphorylation	Kinase	SRC	P12931	PSP
407	Y	Phosphorylation	Kinase	MET	P08581	PSP
407	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
407	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
441	Y	Phosphorylation	Kinase	BMX	P51813	GPS
441	Y	Phosphorylation	Kinase	SRC	P12931	PSP
576	Y	Phosphorylation	Kinase	MET	P08581	PSP
576	Y	Phosphorylation	Kinase	FGR	P09769	PSP
576	Y	Phosphorylation	Kinase	RET	P07949	Uniprot
576	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
576	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
576	Y	Phosphorylation	Kinase	BMX	P51813	GPS
577	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
577	Y	Phosphorylation	Kinase	RET	P07949	Uniprot
577	Y	Phosphorylation	Kinase	MET	P08581	PSP
577	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
577	Y	Phosphorylation	Kinase	BMX	P51813	GPS
695	S	Phosphorylation	Kinase	AKT1	P31749	PSP
700	T	Phosphorylation	Kinase	AKT1	P31749	PSP
732	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
732	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
742	Y	Phosphorylation	Kinase	BMX	P51813	GPS
742	Y	Phosphorylation	Kinase	SRC	P12931	PSP
861	Y	Phosphorylation	Kinase	MET	P08581	PSP
861	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
861	Y	Phosphorylation	Kinase	YES1	P07947	GPS
861	Y	Phosphorylation	Kinase	RET	P07949	PSP
861	Y	Phosphorylation	Kinase	BMX	P51813	GPS
861	Y	Phosphorylation	Kinase	SRC	P12931	PSP
898	Y	Phosphorylation	Kinase	SRC	P12931	PSP
898	Y	Phosphorylation	Kinase	BMX	P51813	GPS
910	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
925	Y	Phosphorylation	Kinase	MET	P08581	PSP
925	Y	Phosphorylation	Kinase	YES1	P07947	GPS
925	Y	Phosphorylation	Kinase	BMX	P51813	GPS
925	Y	Phosphorylation	Kinase	SRC	P12931	PSP
925	Y	Phosphorylation	Kinase	RET	P07949	PSP
925	Y	Phosphorylation	Kinase	FGR	P09769	PSP
1007	Y	Phosphorylation	Kinase	SRC	P12931	PSP
1007	Y	Phosphorylation	Kinase	BMX	P51813	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
722	S	Phosphorylation		19339212
Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRS1_HUMAN	IRS1	physical	9822703
SOCS2_HUMAN	SOCS2	physical	16189514
ATG12_HUMAN	ATG12	physical	16189514
BCAR1_HUMAN	BCAR1	physical	12615911
DOCK1_HUMAN	DOCK1	physical	12615911
SRC_HUMAN	SRC	physical	12615911
CRK_HUMAN	CRK	physical	12615911
JIP3_HUMAN	MAPK8IP3	physical	12226752
EGFR_HUMAN	EGFR	physical	10806474
JAK2_HUMAN	JAK2	physical	9553131
STAT1_HUMAN	STAT1	physical	11278462
TGFI1_HUMAN	TGFB1I1	physical	9422762
PAXI_HUMAN	PXN	physical	9422762
CCR5_HUMAN	CCR5	physical	10384144
CXCR4_HUMAN	CXCR4	physical	11668182
TSC1_HUMAN	TSC1	physical	17043358
TSC2_HUMAN	TSC2	physical	17043358
PTN11_HUMAN	PTPN11	physical	10082579
EPHA2_HUMAN	EPHA2	physical	10655584
PAXI_HUMAN	PXN	physical	11919182
ITA4_HUMAN	ITGA4	physical	11919182
SRC_HUMAN	SRC	physical	12387730
FGR_HUMAN	FGR	physical	12387730
TLN1_HUMAN	TLN1	physical	9442086
PAXI_HUMAN	PXN	physical	9442086
SRC_HUMAN	SRC	physical	12558988
GRB2_HUMAN	GRB2	physical	12558988
AMPH_HUMAN	AMPH	physical	12558988
BIN1_HUMAN	BIN1	physical	12558988
FYN_HUMAN	FYN	physical	12558988
YES_HUMAN	YES1	physical	12558988
CASL_HUMAN	NEDD9	physical	8668148
JAK2_HUMAN	JAK2	physical	10925297
STAT3_HUMAN	STAT3	physical	10925297
PP1B_HUMAN	PPP1CB	physical	11513739
FAK1_HUMAN	PTK2	physical	12005431
KSYK_HUMAN	SYK	physical	9169439
LYN_HUMAN	LYN	physical	9169439
P85A_HUMAN	PIK3R1	physical	7537275
KSYK_HUMAN	SYK	physical	9342235
FYN_HUMAN	FYN	physical	11278857
BCAR1_HUMAN	BCAR1	physical	12135674
BCAR1_HUMAN	BCAR1	physical	10753828
PAXI_HUMAN	PXN	physical	10753828
SRC_HUMAN	SRC	physical	9822703
DCC_HUMAN	DCC	physical	15494733
NEO1_HUMAN	NEO1	physical	15494733
G3P_HUMAN	GAPDH	physical	18206965
PARP1_HUMAN	PARP1	physical	18206965
P53_HUMAN	TP53	physical	18206965
MDM2_HUMAN	MDM2	physical	18206965
SOCS3_HUMAN	SOCS3	physical	18031698
HES1_HUMAN	HES1	physical	21900206
NASP_HUMAN	NASP	physical	21900206
F16P1_HUMAN	FBP1	physical	21900206
F13A_HUMAN	F13A1	physical	21900206
BBS10_HUMAN	BBS10	physical	21900206
NACAD_HUMAN	NACAD	physical	21900206
EF1G_HUMAN	EEF1G	physical	21900206
DX39A_HUMAN	DDX39A	physical	21900206
ZN331_HUMAN	ZNF331	physical	21900206
TGFI1_HUMAN	TGFB1I1	physical	21900206
ES8L2_HUMAN	EPS8L2	physical	21900206
LPXN_HUMAN	LPXN	physical	21900206
DAG1_HUMAN	DAG1	physical	18341635
SH3K1_HUMAN	SH3KBP1	physical	12771190
PDC6I_HUMAN	PDCD6IP	physical	12771190
CBL_HUMAN	CBL	physical	12771190
ASAP1_HUMAN	ASAP1	physical	17893324
BCAR1_HUMAN	BCAR1	physical	21855630
SRC_HUMAN	SRC	physical	21855630
STAP2_HUMAN	STAP2	physical	17675501
CHIP_HUMAN	STUB1	physical	22734001
STAT1_HUMAN	STAT1	physical	20576130
SOCS3_HUMAN	SOCS3	physical	16007195
A4_HUMAN	APP	physical	21832049
PTH2_HUMAN	PTRH2	physical	21383007
SAE1_HUMAN	SAE1	physical	21988832
PAXI_HUMAN	PXN	physical	10980697
TRI72_HUMAN	TRIM72	physical	24344130
UBE2H_HUMAN	UBE2H	physical	24344130
YES_HUMAN	YES1	physical	25416956
SOCS3_HUMAN	SOCS3	physical	25416956
DEFI6_HUMAN	DEF6	physical	25416956
TRM6_HUMAN	TRMT6	physical	26344197
GRB7_HUMAN	GRB7	physical	25814554
HCK_HUMAN	HCK	physical	25814554
PKD1_HUMAN	PKD1	physical	11113628
SRC_HUMAN	SRC	physical	25241761
ERBB2_HUMAN	ERBB2	physical	25241761
P53_HUMAN	TP53	physical	25241761
CCNA1_HUMAN	CCNA1	physical	25241761
PIAS1_HUMAN	PIAS1	physical	25241761
STAT3_HUMAN	STAT3	physical	25241761
RET_HUMAN	RET	physical	25241761
APC_HUMAN	APC	physical	25241761
PTEN_HUMAN	PTEN	physical	9927060
ERBB2_HUMAN	ERBB2	physical	12600989
P85A_HUMAN	PIK3R1	physical	10973983
ITB1_HUMAN	ITGB1	physical	25792870

Drug and Disease Associations

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

Regulatory Network of FAK1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5; THR-13; SER-16;SER-29; THR-386; SER-390; SER-392; THR-394; TYR-397; THR-406; TYR-407;TYR-570; THR-575; TYR-576; TYR-577; SER-580; SER-677; THR-700;SER-702; SER-705; SER-708; SER-716; TYR-720; SER-722; SER-840;SER-843; TYR-861 AND SER-910, PHOSPHORYLATION [LARGE SCALE ANALYSIS]AT TYR-688 (ISOFORM 2), AND MASS SPECTROMETRY.	19369195 [Abstract]
"Specific tyrosine phosphorylation of focal adhesion kinase mediatedby Fer tyrosine kinase in suspended hepatocytes."; Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G.,Oh E.S., Buday L., Kim S.H., Lee J.W.; Biochim. Biophys. Acta 1793:781-791(2009). Cited for: PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 ANDTYR-925, AND IDENTIFICATION IN A COMPLEX WITH CTTN AND FER.	19339212 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-568;TYR-570; SER-722; SER-840; SER-887 AND SER-910, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397; TYR-576; SER-722;SER-840; SER-843 AND SER-910, AND MASS SPECTROMETRY.	17192257 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397 AND SER-840, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain,priming a direct and reciprocal RET-FAK transactivation mechanism."; Plaza-Menacho I., Morandi A., Mologni L., Boender P.,Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P.,McDonald N.Q., Isacke C.M.; J. Biol. Chem. 286:17292-17302(2011). Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, ANDPHOSPHORYLATION AT TYR-576 AND TYR-577.	21454698 [Abstract]
"ZF21 protein regulates cell adhesion and motility."; Nagano M., Hoshino D., Sakamoto T., Kawasaki N., Koshikawa N.,Seiki M.; J. Biol. Chem. 285:21013-21022(2010). Cited for: INTERACTION WITH ZFYVE21, AND DEPHOSPHORYLATION AT TYR-397.	20439989 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-576; TYR-577 ANDTYR-861, AND MASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-576, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Inhibition of both focal adhesion kinase and insulin-like growthfactor-I receptor kinase suppresses glioma proliferation in vitro andin vivo."; Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T.,Jackson D., de Groot J., Yung W.K.; Mol. Cancer Ther. 6:1357-1367(2007). Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, AND PHOSPHORYLATION ATTYR-397.	17431114 [Abstract]
"Cellular characterization of a novel focal adhesion kinaseinhibitor."; Slack-Davis J.K., Martin K.H., Tilghman R.W., Iwanicki M., Ung E.J.,Autry C., Luzzio M.J., Cooper B., Kath J.C., Roberts W.G.,Parsons J.T.; J. Biol. Chem. 282:14845-14852(2007). Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, AND PHOSPHORYLATION ATTYR-397.	17395594 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397; TYR-570; TYR-576;TYR-577 AND TYR-861, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Therapeutic efficacy of a novel focal adhesion kinase inhibitorTAE226 in ovarian carcinoma."; Halder J., Lin Y.G., Merritt W.M., Spannuth W.A., Nick A.M., Honda T.,Kamat A.A., Han L.Y., Kim T.J., Lu C., Tari A.M., Bornmann W.,Fernandez A., Lopez-Berestein G., Sood A.K.; Cancer Res. 67:10976-10983(2007). Cited for: ENZYME REGULATION, ROLE IN DISEASE, AND PHOSPHORYLATION AT TYR-397 ANDTYR-861.	18006843 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-576, AND MASSSPECTROMETRY.	15951569 [Abstract]
"The proto-oncogene Fgr regulates cell migration and this requires itsplasma membrane localization."; Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,Lowell C.A., Berton G.; Exp. Cell Res. 302:253-269(2005). Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, AND PHOSPHORYLATION ATTYR-407; TYR-397 AND TYR-576.	15561106 [Abstract]
"Site-specific phosphorylation of platelet focal adhesion kinase bylow-density lipoprotein."; Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.; Biochem. J. 369:407-416(2003). Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, ANDINTERACTION WITH FGR.	12387730 [Abstract]

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