Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Focal adhesion kinase 1  

UniProtKB / Swiss-Prot ID :  FAK1_HUMAN

Gene Name (Synonyms) : 
PTK2, FAK, FAK1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, centrosome (By similarity). Nucleus. Note=Constituent of focal adhesions. Detected at m 

Protein Function :  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 MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCHHHHCCCCCCCCHHHHHHHHHHHHHCCCCCCCHHHHHHCCCCHHHHHHHHHH...
Protein Variant
LocationDescription
292H -> P. VAR_041682
292H -> Q. VAR_041683
793V -> A (in a glioblastoma multiformesample; somatic mutation).
1030D -> E. VAR_041685
1044K -> E (in a metastatic melanoma sample;somatic mutation).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAYL
---CCCCCC
16.47UniProtKB
Link-
5PhosphotyrosineMAAAYLDPN
CCCCCCCCC
13.60Phosphositeplus
Link-
5Phosphotyrosine.MAAAYLDPN
CCCCCCCCC
13.60UniProtKB
Link-
13PhosphothreonineNLNHTPNSS
CCCCCCCCC
24.08HPRD
Link-
13PhosphothreonineNLNHTPNSS
CCCCCCCCC
24.08Phosphositeplus
Link-
13PhosphothreonineNLNHTPNSS
CCCCCCCCC
24.08SysPTM
Link-
13Phosphothreonine.NLNHTPNSS
CCCCCCCCC
24.08UniProtKB
Link-
16PhosphoserineHTPNSSTKT
CCCCCCCHH
40.36HPRD
Link-
16PhosphoserineHTPNSSTKT
CCCCCCCHH
40.36Phosphositeplus
Link-
16Phosphoserine.HTPNSSTKT
CCCCCCCHH
40.36UniProtKB
Link-
24PhosphothreonineTHLGTGMER
HHHCCCCCC
39.45HPRD
Link-
29PhosphoserineGMERSPGAM
CCCCCCHHH
17.87HPRD
Link-
29PhosphoserineGMERSPGAM
CCCCCCHHH
17.87Phosphositeplus
Link-
29PhosphoserineGMERSPGAM
CCCCCCHHH
17.87SysPTM
Link-
29Phosphoserine.GMERSPGAM
CCCCCCHHH
17.87UniProtKB
Link-
131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)RYLPKGFLN
EECCHHHHH
60.75HPRD
Link-
148PhosphotyrosineLNFFYQQVK
HHHHHHHHH
8.22Phosphositeplus
Link-
155PhosphotyrosineVKSDYMLEI
HHHHHHHHH
15.64Phosphositeplus
Link-
194PhosphotyrosineKKSNYEVLE
CCCCHHHHH
17.95Phosphositeplus
Link-
347PhosphotyrosineLIDGYCRLV
CCCCCCCCC
3.17PhosphoELM
Link-
347PhosphotyrosineLIDGYCRLV
CCCCCCCCC
3.17Phosphositeplus
Link-
386PhosphothreonineQGMRTHAVS
CCCCCCCCC
12.80HPRD
Link-
386Phosphothreonine.QGMRTHAVS
CCCCCCCCC
12.80UniProtKB
Link-
390PhosphoserineTHAVSVSET
CCCCCCCCC
22.25Phosphositeplus
Link-
390Phosphoserine (PTK2)THAVSVSET
CCCCCCCCC
22.25HPRD
Link-
390Phosphoserine.THAVSVSET
CCCCCCCCC
22.25UniProtKB
Link-
392PhosphoserineAVSVSETDD
CCCCCCCCC
27.54Phosphositeplus
Link-
392Phosphoserine.AVSVSETDD
CCCCCCCCC
27.54UniProtKB
Link-
394PhosphothreonineSVSETDDYA
CCCCCCCCC
27.02Phosphositeplus
Link-
394Phosphothreonine.SVSETDDYA
CCCCCCCCC
27.02UniProtKB
Link-
397DePhosphotyrosineETDDYAEII
CCCCCCCCC
14.67HPRD
Link-
397DePhosphotyrosineETDDYAEII
CCCCCCCCC
14.67HPRD
Link-
397PhosphotyrosineETDDYAEII
CCCCCCCCC
14.67HPRD
Link-
397PhosphotyrosineETDDYAEII
CCCCCCCCC
14.67Phosphositeplus
Link-
397PhosphotyrosineETDDYAEII
CCCCCCCCC
14.67SysPTM
Link-
397Phosphotyrosine (CRK)ETDDYAEII
CCCCCCCCC
14.67HPRD
Link-
397Phosphotyrosine (FAK)ETDDYAEII
CCCCCCCCC
14.67PhosphoELM
Link-
397Phosphotyrosine (PTK2)ETDDYAEII
CCCCCCCCC
14.67HPRD
Link-
397Phosphotyrosine; by autocatalysis.ETDDYAEII
CCCCCCCCC
14.67UniProtKB
Link-
406Phosphothreonine.DEEDTYTMP
CCCCCCCCC
24.95UniProtKB
Link-
407PhosphotyrosineEEDTYTMPS
CCCCCCCCC
17.23PhosphoELM
Link-
407PhosphotyrosineEEDTYTMPS
CCCCCCCCC
17.23Phosphositeplus
Link-
407Phosphotyrosine (PTK2B)EEDTYTMPS
CCCCCCCCC
17.23HPRD
Link-
407Phosphotyrosine (SRC)EEDTYTMPS
CCCCCCCCC
17.23HPRD
Link-
407Phosphotyrosine.EEDTYTMPS
CCCCCCCCC
17.23UniProtKB
Link-
408PhosphothreonineEDTYTMPST
CCCCCCCCC
25.38HPRD
Link-
441PhosphotyrosineHQGIYMSPE
EEEEEECCC
9.81Phosphositeplus
Link-
503PhosphothreonineMELCTLGEL
EEECCCCCH
50.88Phosphositeplus
Link-
517PhosphoserineVRKYSLDLA
HCCCCCCHH
20.60Phosphositeplus
Link-
568PhosphoserineDFGLSRYME
ECCEEEEEC
23.03HPRD
Link-
568PhosphoserineDFGLSRYME
ECCEEEEEC
23.03Phosphositeplus
Link-
568PhosphoserineDFGLSRYME
ECCEEEEEC
23.03SysPTM
Link-
568Phosphoserine.DFGLSRYME
ECCEEEEEC
23.03UniProtKB
Link-
570PhosphotyrosineGLSRYMEDS
CEEEEECCC
11.07HPRD
Link-
570PhosphotyrosineGLSRYMEDS
CEEEEECCC
11.07PhosphoELM
Link-
570PhosphotyrosineGLSRYMEDS
CEEEEECCC
11.07Phosphositeplus
Link-
570PhosphotyrosineGLSRYMEDS
CEEEEECCC
11.07SysPTM
Link-
570Phosphotyrosine.GLSRYMEDS
CEEEEECCC
11.07UniProtKB
Link-
574PhosphoserineYMEDSTYYK
EECCCCEEE
12.66Phosphositeplus
Link-
575PhosphothreonineMEDSTYYKA
ECCCCEEEE
43.10Phosphositeplus
Link-
575Phosphothreonine.MEDSTYYKA
ECCCCEEEE
43.10UniProtKB
Link-
576PhosphotyrosineEDSTYYKAS
CCCCEEEEE
13.61Phosphositeplus
Link-
576Phosphotyrosine (FAK)EDSTYYKAS
CCCCEEEEE
13.61PhosphoELM
Link-
576Phosphotyrosine (INSR)EDSTYYKAS
CCCCEEEEE
13.61HPRD
Link-
576Phosphotyrosine (RET)EDSTYYKAS
CCCCEEEEE
13.61HPRD
Link-
576Phosphotyrosine (SRC)EDSTYYKAS
CCCCEEEEE
13.61HPRD
Link-
576Phosphotyrosine; by RET and SRC.EDSTYYKAS
CCCCEEEEE
13.61UniProtKB
Link-
577PhosphotyrosineDSTYYKASK
CCCEEEEEE
10.52HPRD
Link-
577PhosphotyrosineDSTYYKASK
CCCEEEEEE
10.52Phosphositeplus
Link-
577Phosphotyrosine (FAK)DSTYYKASK
CCCEEEEEE
10.52PhosphoELM
Link-
577Phosphotyrosine (INSR)DSTYYKASK
CCCEEEEEE
10.52HPRD
Link-
577Phosphotyrosine (RET)DSTYYKASK
CCCEEEEEE
10.52HPRD
Link-
577Phosphotyrosine (SRC)DSTYYKASK
CCCEEEEEE
10.52HPRD
Link-
577Phosphotyrosine; by RET and SRC.DSTYYKASK
CCCEEEEEE
10.52UniProtKB
Link-
580PhosphoserineYYKASKGKL
EEEEEEECC
37.48Phosphositeplus
Link-
580Phosphoserine.YYKASKGKL
EEEEEEECC
37.48UniProtKB
Link-
677PhosphoserineKAQLSTILE
HHHHHHHHH
11.00Phosphositeplus
Link-
677Phosphoserine.KAQLSTILE
HHHHHHHHH
11.00UniProtKB
Link-
700Phosphothreonine.RRQATVSWD
CCCCCCCCC
13.51UniProtKB
Link-
702PhosphoserineQATVSWDSG
CCCCCCCCC
22.32Phosphositeplus
Link-
702Phosphoserine.QATVSWDSG
CCCCCCCCC
22.32UniProtKB
Link-
704noneTVSWDSGGS
CCCCCCCCC
29.87HPRD
Link-
705PhosphoserineVSWDSGGSD
CCCCCCCCC
38.50HPRD
Link-
705PhosphoserineVSWDSGGSD
CCCCCCCCC
38.50Phosphositeplus
Link-
705Phosphoserine.VSWDSGGSD
CCCCCCCCC
38.50UniProtKB
Link-
708Phosphoserine.DSGGSDEAP
CCCCCCCCC
35.48UniProtKB
Link-
716PhosphoserinePPKPSRPGY
CCCCCCCCC
58.18HPRD
Link-
716Phosphoserine.PPKPSRPGY
CCCCCCCCC
58.18UniProtKB
Link-
720PhosphotyrosineSRPGYPSPR
CCCCCCCCC
11.83Phosphositeplus
Link-
720Phosphotyrosine.SRPGYPSPR
CCCCCCCCC
11.83UniProtKB
Link-
722PhosphoserinePGYPSPRSS
CCCCCCCCC
25.18HPRD
Link-
722PhosphoserinePGYPSPRSS
CCCCCCCCC
25.18PhosphoELM
Link-
722PhosphoserinePGYPSPRSS
CCCCCCCCC
25.18Phosphositeplus
Link-
722PhosphoserinePGYPSPRSS
CCCCCCCCC
25.18SysPTM
Link-
722Phosphoserine.PGYPSPRSS
CCCCCCCCC
25.18UniProtKB
Link-
732PhosphoserineGFYPSPQHM
CCCCCCCCC
26.30Phosphositeplus
Link-
732Phosphoserine (ROCK1)GFYPSPQHM
CCCCCCCCC
26.30PhosphoELM
Link-
732Phosphoserine; by CDK5.GFYPSPQHM
CCCCCCCCC
26.30UniProtKB
Link-
805PhosphothreonineQVLPTHLME
CCCCHHHHH
24.39Phosphositeplus
Link-
840PhosphoserineDVRLSRGSI
CCCCCCCCC
24.83HPRD
Link-
840PhosphoserineDVRLSRGSI
CCCCCCCCC
24.83PhosphoELM
Link-
840PhosphoserineDVRLSRGSI
CCCCCCCCC
24.83Phosphositeplus
Link-
840PhosphoserineDVRLSRGSI
CCCCCCCCC
24.83SysPTM
Link-
840Phosphoserine.DVRLSRGSI
CCCCCCCCC
24.83UniProtKB
Link-
843PhosphoserineLSRGSIDRE
CCCCCCCCC
21.87HPRD
Link-
843PhosphoserineLSRGSIDRE
CCCCCCCCC
21.87PhosphoELM
Link-
843PhosphoserineLSRGSIDRE
CCCCCCCCC
21.87Phosphositeplus
Link-
843Phosphoserine.LSRGSIDRE
CCCCCCCCC
21.87UniProtKB
Link-
850PhosphoserineREDGSLQGP
CCCCCCCCC
29.82Phosphositeplus
Link-
850Phosphoserine (PTK2)REDGSLQGP
CCCCCCCCC
29.82HPRD
Link-
861PhosphotyrosineNQHIYQPVG
CCCCCCCCC
12.49HPRD
Link-
861PhosphotyrosineNQHIYQPVG
CCCCCCCCC
12.49Phosphositeplus
Link-
861Phosphotyrosine (SRC)NQHIYQPVG
CCCCCCCCC
12.49HPRD
Link-
861Phosphotyrosine (SRC;SRC)NQHIYQPVG
CCCCCCCCC
12.49PhosphoELM
Link-
861Phosphotyrosine.NQHIYQPVG
CCCCCCCCC
12.49UniProtKB
Link-
887PhosphoserineGHLGSLASL
CCCCCCCCC
27.42HPRD
Link-
887PhosphoserineGHLGSLASL
CCCCCCCCC
27.42Phosphositeplus
Link-
887PhosphoserineGHLGSLASL
CCCCCCCCC
27.42SysPTM
Link-
887Phosphoserine.GHLGSLASL
CCCCCCCCC
27.42UniProtKB
Link-
892PhosphoserineLASLSSPAD
CCCCCCCCC
31.61HPRD
Link-
892PhosphoserineLASLSSPAD
CCCCCCCCC
31.61PhosphoELM
Link-
910PhosphoserinePQEISPPPT
CEECCCCCC
30.51HPRD
Link
910PhosphoserinePQEISPPPT
CEECCCCCC
30.51PhosphoELM
Link
910PhosphoserinePQEISPPPT
CEECCCCCC
30.51Phosphositeplus
Link
910PhosphoserinePQEISPPPT
CEECCCCCC
30.51SysPTM
Link
910Phosphoserine.PQEISPPPT
CEECCCCCC
30.51UniProtKB
Link
914PhosphothreonineSPPPTANLD
CCCCCCCCC
33.67HPRD
Link
914PhosphothreonineSPPPTANLD
CCCCCCCCC
33.67Phosphositeplus
Link
925PhosphotyrosineNDKVYENVT
CCCEEHHHH
13.92PhosphoELM
Link
925PhosphotyrosineNDKVYENVT
CCCEEHHHH
13.92Phosphositeplus
Link
925Phosphotyrosine (PTK2)NDKVYENVT
CCCEEHHHH
13.92HPRD
Link
925Phosphotyrosine (SRC)NDKVYENVT
CCCEEHHHH
13.92HPRD
Link
925Phosphotyrosine.NDKVYENVT
CCCEEHHHH
13.92UniProtKB
Link
1007PhosphotyrosineLAQQYVMTS
HHHHHHHHH
4.70Phosphositeplus
Link
1016PhosphotyrosineLQQEYKKQM
HHHHHHHHH
21.10HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LYN_HUMANphysical interactionMINT-17602MINT11389892
BCAR1_HUMANphysical interactionMINT-74938MINT9285683
P53_HUMANdirect interaction
direct interaction
direct interaction
physical interaction
colocalization
colocalization
physical interaction
EBI-1544705
EBI-1544471
EBI-1
intact15855171
15855171
15855171
15855171
15855171
15855171
15855171
15855171
15855171
15855171
15855171
SRC_HUMANphysical interactionEBI-968957
intact16291744
ACTN1_HUMANin vivoHPRD:02859HPRD11369769
GRB2_HUMANin vitro
in vivo
HPRD:02859HPRD7997267
EZRI_HUMANin vitro
in vivo
HPRD:02859HPRD11468295
CSK_HUMANin vitro
in vivo
HPRD:02859HPRD7529872
LYAM2_HUMANin vitroHPRD:02859HPRD8609175
EGFR_HUMANin vitro
in vivo
HPRD:02859HPRD10806474
FYN_HUMANin vitroHPRD:02859HPRD11278857
ITB1_HUMANin vitroHPRD:02859HPRD8649427
IRS1_HUMANyeast 2-hybridHPRD:02859HPRD9822703
JAK2_HUMANin vivoHPRD:02859HPRD9553131
10925297
PLCG1_HUMANin vitro
in vivo
HPRD:02859HPRD8660853
10430888
PGFRB_HUMANin vitro
in vivo
HPRD:02859HPRD10806474
ITB3_HUMANin vitro
in vivo
HPRD:02859HPRD8649427
ERBB2_HUMANin vivoHPRD:02859HPRD11807823
APC_HUMANin vivoHPRD:02859HPRD7744883
FGR_HUMANin vivoHPRD:02859HPRD12387730
LYN_HUMANin vivoHPRD:02859HPRD11389892
PTN11_HUMANin vitro
in vivo
HPRD:02859HPRD10655584
7589239
8986614
10082579
EPHA2_HUMANin vivoHPRD:02859HPRD10655584
P85A_HUMANin vivoHPRD:02859HPRD7537275
8649427
10806474
ERBB3_HUMANin vivoHPRD:02859HPRD11807823
BMX_HUMANin vitro
in vivo
HPRD:02859HPRD11331870
ITB2_HUMANin vitroHPRD:02859HPRD8649427
TLN1_HUMANin vitro
in vivo
HPRD:02859HPRD7622520
ITAV_HUMANin vitroHPRD:02859HPRD11927607
KSYK_HUMANin vivoHPRD:02859HPRD9342235
9169439
PAXI_HUMANin vitro
in vivo
HPRD:02859HPRD9658172
11337490
9230116
STAT1_HUMANin vitro
in vivo
HPRD:02859HPRD11278462
SHC1_HUMANin vitro
in vivo
HPRD:02859HPRD11980671
FAK1_HUMANin vitro
in vivo
HPRD:02859HPRD7529876
11314030
7509446
12370821
8816475
7997267
TRIO_HUMANin vitro
in vivo
HPRD:02859HPRD12551902
BCAR1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02859HPRD11514617
7479864
9360983
12119061
9360968
VGFR1_HUMANin vivoHPRD:02859HPRD12023386
VINC_HUMANin vivoHPRD:02859HPRD10545505
RIPK1_HUMANin vitro
in vivo
HPRD:02859HPRD15121855
SOCS2_HUMANyeast 2-hybridHPRD:02859HPRD16189514
ATG12_HUMANyeast 2-hybridHPRD:02859HPRD16189514
ROCK1_HUMANin vitroHPRD:02859HPRD15247219
P53_HUMANin vitro
in vivo
HPRD:02859HPRD15855171
ITA3_HUMANENSP00000341189STRING
BCAR1_HUMANENSP00000341189STRING
ITB4_HUMANENSP00000341189STRING
TRIP6_HUMANENSP00000341189STRING
VINC_HUMANENSP00000341189STRING
MK01_HUMANENSP00000341189STRING
CSK_HUMANENSP00000341189STRING
P85B_HUMANENSP00000341189STRING
HGF_HUMANENSP00000341189STRING
GIT1_HUMANENSP00000341189STRING
CCND1_HUMANENSP00000341189STRING
PAXI_HUMANENSP00000341189STRING
NCK2_HUMANENSP00000341189STRING
ELAF_HUMANENSP00000341189STRING
CDN1A_HUMANENSP00000341189STRING
PTN12_HUMANENSP00000341189STRING
PIAS1_HUMANENSP00000341189STRING
INS_HUMANENSP00000341189STRING
INS_HUMANENSP00000341189STRING
ITAV_HUMANENSP00000341189STRING
PGFRB_HUMANENSP00000341189STRING
NEO1_HUMANENSP00000341189STRING
ITB3_HUMANENSP00000341189STRING
MK03_HUMANENSP00000341189STRING
FARP2_HUMANENSP00000341189STRING
TBB4_HUMANENSP00000341189STRING
P3C2G_HUMANENSP00000341189STRING
P53_HUMANENSP00000341189STRING
ERBB2_HUMANENSP00000341189STRING
KPYR_HUMANENSP00000341189STRING
P85A_HUMANENSP00000341189STRING
RASA1_HUMANENSP00000341189STRING
EGFR_HUMANENSP00000341189STRING
CAN1_HUMANENSP00000341189STRING
VGFR1_HUMANENSP00000341189STRING
KPCA_HUMANENSP00000341189STRING
ITB5_HUMANENSP00000341189STRING
CDK5_HUMANENSP00000341189STRING
CRK_HUMANENSP00000341189STRING
CRK_HUMANENSP00000341189STRING
ITB2_HUMANENSP00000341189STRING
DCC_HUMANENSP00000341189STRING
IRS1_HUMANENSP00000341189STRING
RASH_HUMANENSP00000341189STRING
GRB7_HUMANENSP00000341189STRING
CDC42_HUMANENSP00000341189STRING
KLF8_HUMANENSP00000341189STRING
VEGFA_HUMANENSP00000341189STRING
APOA_HUMANENSP00000341189STRING
FAK2_HUMANENSP00000341189STRING
ZYX_HUMANENSP00000341189STRING
DDEF1_HUMANENSP00000341189STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
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