FAK2_MOUSE - dbPTM
FAK2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAK2_MOUSE
UniProt AC Q9QVP9
Protein Name Protein-tyrosine kinase 2-beta
Gene Name Ptk2b
Organism Mus musculus (Mouse).
Sequence Length 1009
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium. Cytoplasm, cell cortex. Nucleus. Colocalizes with integrins at the cell periphery (
Protein Description Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. 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 of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 (By similarity)..
Protein Sequence MSGVSEPLSRVKVGTLRRPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIKSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIMHAKKDGEKRNSLPQIPTLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGVAREEVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTQDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVPTLVLYTLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMEKDIAIEQERNARYRPPKILEPTTFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAEKIKMKQVLERQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYHNVMTLVEAVLELKNKLGQLPPEDYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMKLAQQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSGVSEPLS
------CCCCCCCCC		60.2430635358
5Phosphorylation---MSGVSEPLSRVK
---CCCCCCCCCCCE		36.7023737553
9PhosphorylationSGVSEPLSRVKVGTL
CCCCCCCCCCEEECC		45.8223737553
15PhosphorylationLSRVKVGTLRRPEGP
CCCCEEECCCCCCCC		21.7826824392
162PhosphorylationYQQLRNDYMQRYASK
HHHHHHHHHHHHHHH		9.9428576409
166PhosphorylationRNDYMQRYASKVSEG
HHHHHHHHHHHCCHH		9.8026643407
168PhosphorylationDYMQRYASKVSEGMA
HHHHHHHHHCCHHHH		25.3426643407
171PhosphorylationQRYASKVSEGMALQL
HHHHHHCCHHHHHHH		31.9726643407
361PhosphorylationLQGEHKGSLIMHAKK
CCCCCCCCEEEEECC		21.37-
375PhosphorylationKDGEKRNSLPQIPTL
CCCCCCCCCCCCCCC		45.5224925903
381PhosphorylationNSLPQIPTLNLEARR
CCCCCCCCCCHHHHH		29.8828833060
389PhosphorylationLNLEARRSHLSESCS
CCHHHHHHHCCCCCC		24.1929899451
392PhosphorylationEARRSHLSESCSIES
HHHHHHCCCCCCCCC		23.2629899451
394PhosphorylationRRSHLSESCSIESDI
HHHHCCCCCCCCCCE		15.1325367039
396PhosphorylationSHLSESCSIESDIYA
HHCCCCCCCCCCEEE		38.3729899451
399PhosphorylationSESCSIESDIYAEIP
CCCCCCCCCEEEECC		27.8629899451
402PhosphorylationCSIESDIYAEIPDET
CCCCCCEEEECCCHH		11.8120442405
418PhosphorylationRRPGGPQYGVAREEV
CCCCCCCCCCCHHHH		19.3925367039
440PhosphorylationEGFFGEVYEGVYTNH
CCCCCEEEEEEEECC		11.5822817900
571PhosphorylationKLGDFGLSRYIEDED
ECCCCCCCCCCCCCC		24.3422817900
573PhosphorylationGDFGLSRYIEDEDYY
CCCCCCCCCCCCCCH		12.8020116462
579PhosphorylationRYIEDEDYYKASVTR
CCCCCCCCHHEECEE		12.5725521595
580PhosphorylationYIEDEDYYKASVTRL
CCCCCCCHHEECEEC		16.6425521595
583PhosphorylationDEDYYKASVTRLPIK
CCCCHHEECEECCCC		21.6222324799
585PhosphorylationDYYKASVTRLPIKWM
CCHHEECEECCCCCC		24.8025367039
722PhosphorylationPKPSRPKYRPPPQTN
CCCCCCCCCCCCCCC		30.9125159016
746PhosphorylationVPEGLCASSPTLTSP
CCCCCCCCCCCCCCC		35.5327087446
747PhosphorylationPEGLCASSPTLTSPM
CCCCCCCCCCCCCCC		11.9021659605
749PhosphorylationGLCASSPTLTSPMEY
CCCCCCCCCCCCCCC		44.6126160508
751PhosphorylationCASSPTLTSPMEYPS
CCCCCCCCCCCCCCC		33.0126160508
752PhosphorylationASSPTLTSPMEYPSP
CCCCCCCCCCCCCCC		25.9226160508
756PhosphorylationTLTSPMEYPSPVNSL
CCCCCCCCCCCCCCC		11.6221659605
758PhosphorylationTSPMEYPSPVNSLHT
CCCCCCCCCCCCCCC		40.3521659605
762PhosphorylationEYPSPVNSLHTPPLH
CCCCCCCCCCCCCCC		23.0527087446
765PhosphorylationSPVNSLHTPPLHRHN
CCCCCCCCCCCCCCC		31.7127087446
778PhosphorylationHNVFKRHSMREEDFI
CCCHHHHCCCHHHCC		24.4623684622
834PhosphorylationRCLDPMVYMNDKSPL
HHCCCEEECCCCCCC		5.5025367039
839PhosphorylationMVYMNDKSPLTPEKE
EEECCCCCCCCCCHH		28.1825367039
842PhosphorylationMNDKSPLTPEKEAGY
CCCCCCCCCCHHCCC		32.5528725479
849PhosphorylationTPEKEAGYTEFTGPP
CCCHHCCCCCCCCCC		15.3318515860
850PhosphorylationPEKEAGYTEFTGPPQ
CCHHCCCCCCCCCCC		24.5725521595
853PhosphorylationEAGYTEFTGPPQKPP
HCCCCCCCCCCCCCC		42.4125367039
866PhosphorylationPPRLGAQSIQPTANL
CCCCCCCCCCCCCCC		23.74-
881PhosphorylationDRTDDLVYHNVMTLV
CCCCCHHHHHHHHHH		8.5815705590
956AcetylationDLAELINKMKLAQQN
HHHHHHHHHHHHHHH		30.342416637
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
402YPhosphorylationKinasePTK2BQ9QVP9
GPS
402YPhosphorylationKinaseSRCP05480
PSP
579YPhosphorylationKinaseLCKP06240
GPS
579YPhosphorylationKinaseLYNP25911
GPS
579YPhosphorylationKinaseSRCP05480
GPS
580YPhosphorylationKinaseFYNP39688
Uniprot
580YPhosphorylationKinaseLCKP06240
Uniprot
580YPhosphorylationKinaseLYNP25911
GPS
580YPhosphorylationKinaseSRCP05480
Uniprot
881YPhosphorylationKinaseSRCP05480
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAK2_MOUSE !!
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 FAK2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC_MOUSESrcphysical
14739300
DOK1_MOUSEDok1physical
10823839
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FAK2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY.
"Hypophosphorylated and inactive Pyk2 associates with paxillin at themicrotubule organizing center in hematopoietic cells.";
St-Pierre J., Lysechko T.L., Ostergaard H.L.;
Cell. Signal. 23:718-730(2011).
Cited for: INTERACTION WITH PXN, SUBCELLULAR LOCATION, AND PHOSPHORYLATION ATTYR-402; TYR-580 AND TYR-881.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-440, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; TYR-579 ANDTYR-580, AND MASS SPECTROMETRY.
"Src kinase activity is essential for osteoclast function.";
Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.;
J. Biol. Chem. 279:17660-17666(2004).
Cited for: FUNCTION IN BONE RESORPTION, INTERACTION WITH SRC, PHOSPHORYLATION ATTYR-402, AND MUTAGENESIS OF TYR-402.
"Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggersphosphorylation of Pyk2.";
Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.;
Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001).
Cited for: PHOSPHORYLATION AT TYR-402, AND INTERACTION WITH NPHP1.
"Different modes and qualities of tyrosine phosphorylation of Fak andPyk2 during epithelial-mesenchymal transdifferentiation and cellmigration: analysis of specific phosphorylation events using site-directed antibodies.";
Nakamura K., Yano H., Schaefer E., Sabe H.;
Oncogene 20:2626-2635(2001).
Cited for: PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.

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