FERM2_MOUSE - dbPTM
FERM2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FERM2_MOUSE
UniProt AC Q8CIB5
Protein Name Fermitin family homolog 2
Gene Name Fermt2
Organism Mus musculus (Mouse).
Sequence Length 680
Subcellular Localization Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Membrane
Peripheral membrane protein
Cytoplasmic side. Cell projection, lamellipodium membrane
Peripheral membrane protein
Cytoplasmic side. Nucleus. Cytoplasm,
Protein Description Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling..
Protein Sequence MALDGIRMPDGCYADGTWELSVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKCGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLIMPGSGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPVTSPEILAKMFKPQALLDKAKTNQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWALLLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSREESSGTPAHQLNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPDQITTDVNPECLVSPRYLKKYKSKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKREELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV
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
81AcetylationKTHWTLDKCGIQADA
HCCEEHHHCCCCCCC		37.1622826441
121AcetylationNFSDRVFKAVSDICK
ECHHHHHHHHHHHHH		45.0522826441
128UbiquitinationKAVSDICKTFNIRHP
HHHHHHHHHCCCCCH		57.39-
128AcetylationKAVSDICKTFNIRHP
HHHHHHHHHCCCCCH		57.3922826441
159PhosphorylationKKKLDDQSEDEALEL
CCCCCCCCHHHHHHH		54.7526824392
175PhosphorylationGPLIMPGSGSIYSSP
CCEECCCCCCCCCCC		24.4025619855
177PhosphorylationLIMPGSGSIYSSPGL
EECCCCCCCCCCCCC		21.7625619855
179PhosphorylationMPGSGSIYSSPGLYS
CCCCCCCCCCCCCCC		12.5625619855
180PhosphorylationPGSGSIYSSPGLYSK
CCCCCCCCCCCCCCC		28.5225619855
181PhosphorylationGSGSIYSSPGLYSKT
CCCCCCCCCCCCCCC		13.1525619855
185PhosphorylationIYSSPGLYSKTMTPT
CCCCCCCCCCCCCCC		17.6525619855
186PhosphorylationYSSPGLYSKTMTPTY
CCCCCCCCCCCCCCC		27.0525619855
188PhosphorylationSPGLYSKTMTPTYDA
CCCCCCCCCCCCCCC		21.9729899451
190PhosphorylationGLYSKTMTPTYDAHD
CCCCCCCCCCCCCCC		20.0826060331
192PhosphorylationYSKTMTPTYDAHDGS
CCCCCCCCCCCCCCC		25.5223649490
193PhosphorylationSKTMTPTYDAHDGSP
CCCCCCCCCCCCCCC		16.6129899451
199PhosphorylationTYDAHDGSPLSPTSA
CCCCCCCCCCCCCCC		28.8226239621
202PhosphorylationAHDGSPLSPTSAWFG
CCCCCCCCCCCCCCC		29.5221183079
214PhosphorylationWFGDSALSEGNPGIL
CCCCHHHCCCCCCEE		43.0823649490
245AcetylationKPQALLDKAKTNQGW
CHHHHHHHHHHCCCH		52.3215615049
247UbiquitinationQALLDKAKTNQGWLD
HHHHHHHHHCCCHHH		54.47-
247AcetylationQALLDKAKTNQGWLD
HHHHHHHHHCCCHHH		54.4715615057
265UbiquitinationSLMEQDVKENEALLL
HHHHHCHHHCHHHHH		64.21-
275UbiquitinationEALLLRFKYYSFFDL
HHHHHHEEEEECCCC		36.52-
285UbiquitinationSFFDLNPKYDAIRIN
ECCCCCCCCCEEHHH		55.48-
285AcetylationSFFDLNPKYDAIRIN
ECCCCCCCCCEEHHH		55.4822826441
328PhosphorylationQYHINKLSIMTSENH
HHHHHHHHHHCCCCC		16.3626239621
331PhosphorylationINKLSIMTSENHLNN
HHHHHHHCCCCCCCC		31.0826239621
332PhosphorylationNKLSIMTSENHLNNS
HHHHHHCCCCCCCCC		21.0126239621
339PhosphorylationSENHLNNSDKEVDEV
CCCCCCCCCCHHHHH		49.3226824392
351PhosphorylationDEVDAALSDLEITLE
HHHHHHHHCEEEEEE		35.1126824392
393MalonylationKLTLKGYKQYWCTFK
EEEECCCEEEEEEEE		45.6526320211
393AcetylationKLTLKGYKQYWCTFK
EEEECCCEEEEEEEE		45.6522826441
400AcetylationKQYWCTFKDTSISCY
EEEEEEEECCEEEEE		41.7822826441
408MalonylationDTSISCYKSREESSG
CCEEEEEECCCCCCC		47.5726320211
409PhosphorylationTSISCYKSREESSGT
CEEEEEECCCCCCCC		20.60-
413PhosphorylationCYKSREESSGTPAHQ
EEECCCCCCCCCCCE		29.3425293948
414PhosphorylationYKSREESSGTPAHQL
EECCCCCCCCCCCEE		50.3825293948
416PhosphorylationSREESSGTPAHQLNL
CCCCCCCCCCCEEEC		21.1725293948
426S-nitrosylationHQLNLRGCEVTPDVN
CEEECCCCEECCCCC		2.8421278135
426S-nitrosocysteineHQLNLRGCEVTPDVN
CEEECCCCEECCCCC		2.84-
550PhosphorylationHQNVAQMSLIEAKMR
HHHHHHHHHHHHHHH		17.7026824392
555UbiquitinationQMSLIEAKMRFIQAW
HHHHHHHHHHHHHHH		20.16-
606PhosphorylationSTGDAIKTWRFSNMK
CCCHHHHEEEECCCC		18.7625338131
666PhosphorylationRAKDQNESLDEEMFY
CCCCCCCCCCHHHHH		48.9825521595
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

Oops, there are no upstream regulatory protein records of FERM2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FERM2_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 FERM2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FERM2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FERM2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-159, AND MASSSPECTROMETRY.

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