FERM2_HUMAN - dbPTM
FERM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FERM2_HUMAN
UniProt AC Q96AC1
Protein Name Fermitin family homolog 2
Gene Name FERMT2
Organism Homo sapiens (Human).
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 MALDGIRMPDGCYADGTWELSVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLITPGSGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPITSPEILAKMFKPQALLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPEQITTDITPECLVSPRYLKKYKNKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKKEELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV
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
13 (in isoform 3)Phosphorylation-17.1627642862
32PhosphorylationTDLNRDVTLRVTGEV
EECCCCEEEEEECEE		17.0924719451
32 (in isoform 3)Phosphorylation-17.0924719451
36PhosphorylationRDVTLRVTGEVHIGG
CCEEEEEECEEEECH		22.61-
51UbiquitinationVMLKLVEKLDVKKDW
HHHHHHHHCCCCCCC		42.37-
56AcetylationVEKLDVKKDWSDHAL
HHHCCCCCCCCCCCH		65.3619828449
59PhosphorylationLDVKKDWSDHALWWE
CCCCCCCCCCCHHHH		29.65-
67UbiquitinationDHALWWEKKRTWLLK
CCCHHHHHHCEEEHH		33.56-
68AcetylationHALWWEKKRTWLLKT
CCHHHHHHCEEEHHC		43.4719828459
81UbiquitinationKTHWTLDKYGIQADA
HCCEEEHHHCCCCCC		48.79-
81 (in isoform 3)Malonylation-48.7930639696
89UbiquitinationYGIQADAKLQFTPQH
HCCCCCCEEEECCCC		43.28-
97UbiquitinationLQFTPQHKLLRLQLP
EEECCCCCEEEEECC		43.92-
107UbiquitinationRLQLPNMKYVKVKVN
EEECCCCCEEEEEEE		54.23-
118MethylationVKVNFSDRVFKAVSD
EEEECHHHHHHHHHH		34.28115481333
128UbiquitinationKAVSDICKTFNIRHP
HHHHHHHHHCCCCCH		57.39-
129PhosphorylationAVSDICKTFNIRHPE
HHHHHHHHCCCCCHH		19.94-
139PhosphorylationIRHPEELSLLKKPRD
CCCHHHHHHCCCCCC		34.6324719451
142UbiquitinationPEELSLLKKPRDPTK
HHHHHHCCCCCCCCH		67.06-
154UbiquitinationPTKKKKKKLDDQSED
CCHHHCCCCCCCCHH		67.06-
159PhosphorylationKKKLDDQSEDEALEL
CCCCCCCCHHHHHHH		54.7522167270
159 (in isoform 2)Phosphorylation-54.7521406692
159 (in isoform 3)Phosphorylation-54.7524719451
172PhosphorylationELEGPLITPGSGSIY
HHCCCEECCCCCCCC		29.3121945579
175PhosphorylationGPLITPGSGSIYSSP
CCEECCCCCCCCCCC		30.4821945579
175 (in isoform 3)Phosphorylation-30.4827642862
177PhosphorylationLITPGSGSIYSSPGL
EECCCCCCCCCCCCC		21.7621945579
177 (in isoform 3)Phosphorylation-21.7624719451
179PhosphorylationTPGSGSIYSSPGLYS
CCCCCCCCCCCCCCC		12.5621945579
179 (in isoform 3)Phosphorylation-12.5627642862
180PhosphorylationPGSGSIYSSPGLYSK
CCCCCCCCCCCCCCC		28.5221945579
180 (in isoform 3)Phosphorylation-28.5227642862
181PhosphorylationGSGSIYSSPGLYSKT
CCCCCCCCCCCCCCC		13.1521945579
181 (in isoform 3)Phosphorylation-13.1527642862
185PhosphorylationIYSSPGLYSKTMTPT
CCCCCCCCCCCCCCC		17.6521945579
185 (in isoform 3)Phosphorylation-17.6527642862
186PhosphorylationYSSPGLYSKTMTPTY
CCCCCCCCCCCCCCC		27.0521945579
186 (in isoform 3)Phosphorylation-27.0527642862
188PhosphorylationSPGLYSKTMTPTYDA
CCCCCCCCCCCCCCC		21.9720068231
190PhosphorylationGLYSKTMTPTYDAHD
CCCCCCCCCCCCCCC		20.0820068231
192PhosphorylationYSKTMTPTYDAHDGS
CCCCCCCCCCCCCCC		25.5220068231
193PhosphorylationSKTMTPTYDAHDGSP
CCCCCCCCCCCCCCC		16.6125884760
199PhosphorylationTYDAHDGSPLSPTSA
CCCCCCCCCCCCCCC		28.8225106551
199 (in isoform 3)Phosphorylation-28.8227251275
202PhosphorylationAHDGSPLSPTSAWFG
CCCCCCCCCCCCCCC		29.5225106551
202 (in isoform 3)Phosphorylation-29.5227251275
204PhosphorylationDGSPLSPTSAWFGDS
CCCCCCCCCCCCCCH		27.9228387310
205PhosphorylationGSPLSPTSAWFGDSA
CCCCCCCCCCCCCHH		27.2126074081
211PhosphorylationTSAWFGDSALSEGNP
CCCCCCCHHHCCCCC		31.3320068231
214PhosphorylationWFGDSALSEGNPGIL
CCCCHHHCCCCCCEE		43.0828464451
224PhosphorylationNPGILAVSQPITSPE
CCCEEEEECCCCCHH		25.3220068231
228PhosphorylationLAVSQPITSPEILAK
EEEECCCCCHHHHHH		44.9320068231
229PhosphorylationAVSQPITSPEILAKM
EEECCCCCHHHHHHH		22.6620068231
236SulfoxidationSPEILAKMFKPQALL
CHHHHHHHHCHHHHH		4.3131801345
238UbiquitinationEILAKMFKPQALLDK
HHHHHHHCHHHHHHH		32.49-
245UbiquitinationKPQALLDKAKINQGW
CHHHHHHHHHCCCHH		52.10-
247UbiquitinationQALLDKAKINQGWLD
HHHHHHHHCCCHHHH		48.18-
258PhosphorylationGWLDSSRSLMEQDVK
HHHHHCHHHHHHCHH		33.73-
260SulfoxidationLDSSRSLMEQDVKEN
HHHCHHHHHHCHHHC		4.6030846556
285UbiquitinationSFFDLNPKYDAIRIN
ECCCCCCCCCEEHHH		55.4821890473
285AcetylationSFFDLNPKYDAIRIN
ECCCCCCCCCEEHHH		55.4823236377
285UbiquitinationSFFDLNPKYDAIRIN
ECCCCCCCCCEEHHH		55.482189047
285 (in isoform 1)Ubiquitination-55.4821890473
285 (in isoform 2)Ubiquitination-55.4821890473
328PhosphorylationQYHINKLSIMTSENH
HHHHHHHHHHCCCCC		16.3620873877
331PhosphorylationINKLSIMTSENHLNN
HHHHHHHCCCCCCCC		31.0820873877
332PhosphorylationNKLSIMTSENHLNNS
HHHHHHCCCCCCCCC		21.0122496350
332 (in isoform 2)Phosphorylation-21.0121406692
339PhosphorylationSENHLNNSDKEVDEV
CCCCCCCCCCHHHHH		49.3229255136
339 (in isoform 2)Phosphorylation-49.3221406692
339 (in isoform 3)Phosphorylation-49.3227251275
351PhosphorylationDEVDAALSDLEITLE
HHHHHHHHCEEEEEE		35.1119664994
351 (in isoform 2)Phosphorylation-35.1121406692
356PhosphorylationALSDLEITLEGGKTS
HHHCEEEEEECCCEE		14.9129632367
362PhosphorylationITLEGGKTSTILGDI
EEEECCCEEEEECCC		34.0828857561
363PhosphorylationTLEGGKTSTILGDIT
EEECCCEEEEECCCC		19.5526657352
364PhosphorylationLEGGKTSTILGDITS
EECCCEEEEECCCCC		26.0028857561
370PhosphorylationSTILGDITSIPELAD
EEEECCCCCCHHHHH		25.9126657352
371PhosphorylationTILGDITSIPELADY
EEECCCCCCHHHHHH		36.1628348404
378PhosphorylationSIPELADYIKVFKPK
CCHHHHHHHHHHCCC		9.31-
388PhosphorylationVFKPKKLTLKGYKQY
HHCCCEEEECCCEEE		34.9924719451
388 (in isoform 3)Phosphorylation-34.9924719451
390UbiquitinationKPKKLTLKGYKQYWC
CCCEEEECCCEEEEE		55.76-
393AcetylationKLTLKGYKQYWCTFK
EEEECCCEEEEEEEE		45.6526051181
393MalonylationKLTLKGYKQYWCTFK
EEEECCCEEEEEEEE		45.6526320211
393 (in isoform 3)Malonylation-45.6526320211
395PhosphorylationTLKGYKQYWCTFKDT
EECCCEEEEEEEECC		9.78-
403PhosphorylationWCTFKDTSISCYKSK
EEEEECCEEEEECCC		23.7221712546
408AcetylationDTSISCYKSKEESSG
CCEEEEECCCCCCCC		60.4226051181
410UbiquitinationSISCYKSKEESSGTP
EEEEECCCCCCCCCC		62.44-
414PhosphorylationYKSKEESSGTPAHQM
ECCCCCCCCCCCCCC		50.3825159151
416PhosphorylationSKEESSGTPAHQMNL
CCCCCCCCCCCCCCC		21.1725159151
421SulfoxidationSGTPAHQMNLRGCEV
CCCCCCCCCCCCCEE		3.5130846556
424MethylationPAHQMNLRGCEVTPD
CCCCCCCCCCEECCC		42.59115481325
426S-palmitoylationHQMNLRGCEVTPDVN
CCCCCCCCEECCCCC		2.8429575903
429PhosphorylationNLRGCEVTPDVNISG
CCCCCEECCCCCCCC		7.4721815630
435PhosphorylationVTPDVNISGQKFNIK
ECCCCCCCCCEEEEE		29.9321712546
438MalonylationDVNISGQKFNIKLLI
CCCCCCCEEEEEEEE		43.8526320211
438UbiquitinationDVNISGQKFNIKLLI
CCCCCCCEEEEEEEE		43.85-
438 (in isoform 3)Malonylation-43.8526320211
451SulfoxidationLIPVAEGMNEIWLRC
EEECCCCCCEEEEEE		2.8330846556
462AcetylationWLRCDNEKQYAHWMA
EEEECCHHHHHHHHH		55.6626051181
479PhosphorylationRLASKGKTMADSSYN
HHHHCCCCCCCCCCC		26.6823322592
484PhosphorylationGKTMADSSYNLEVQN
CCCCCCCCCCHHHHH		20.7023322592
494PhosphorylationLEVQNILSFLKMQHL
HHHHHHHHHHHHCCC		25.4124719451
498SulfoxidationNILSFLKMQHLNPDP
HHHHHHHHCCCCCCC		3.1030846556
523PhosphorylationITPECLVSPRYLKKY
CCHHHCCCHHHHHHH		7.2425159151
523 (in isoform 2)Phosphorylation-7.2425159151
523 (in isoform 3)Phosphorylation-7.2425159151
528UbiquitinationLVSPRYLKKYKNKQI
CCCHHHHHHHCCCHH		45.16-
533UbiquitinationYLKKYKNKQITARIL
HHHHHCCCHHHHHHH		38.64-
536PhosphorylationKYKNKQITARILEAH
HHCCCHHHHHHHHHH		13.8522964224
549SulfoxidationAHQNVAQMSLIEAKM
HHHHHHHHHHHHHHH		2.2530846556
550PhosphorylationHQNVAQMSLIEAKMR
HHHHHHHHHHHHHHH		17.7022964224
555AcetylationQMSLIEAKMRFIQAW
HHHHHHHHHHHHHHH		20.1627452117
582UbiquitinationARFQGGKKEELIGIA
HHCCCCCHHHHHHHH		60.75-
590PhosphorylationEELIGIAYNRLIRMD
HHHHHHHHHHHHCCC		10.0126657352
596SulfoxidationAYNRLIRMDASTGDA
HHHHHHCCCCCCCHH		3.9130846556
597 (in isoform 3)Phosphorylation-27.7627251275
605AcetylationASTGDAIKTWRFSNM
CCCCHHHHEEEECCC		43.7027452117
605UbiquitinationASTGDAIKTWRFSNM
CCCCHHHHEEEECCC		43.70-
606PhosphorylationSTGDAIKTWRFSNMK
CCCHHHHEEEECCCC		18.7628857561
610PhosphorylationAIKTWRFSNMKQWNV
HHHEEEECCCCCCEE		27.6923403867
617 (in isoform 3)Phosphorylation-8.8627251275
623SulfoxidationNVNWEIKMVTVEFAD
EEEEEEEEEEEEECC		3.6228183972
633 (in isoform 2)Phosphorylation-23.67-
666PhosphorylationRAKDQNESLDEEMFY
CCCCCCCCCCHHHHH		48.9819664994
671SulfoxidationNESLDEEMFYKLTSG
CCCCCHHHHHHHHHC		4.1230846556
673PhosphorylationSLDEEMFYKLTSGWV
CCCHHHHHHHHHCCC		12.0922167270
673 (in isoform 3)Phosphorylation-12.0924719451
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
159SPhosphorylationKinaseIKKEQ14164
PSP
193YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FERM2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBLI1_HUMANFBLIM1physical
12679033
A4_HUMANAPPphysical
21832049
SEPT9_HUMANSEPT9physical
22939629
SEP11_HUMANSEPT11physical
22939629
ZYX_HUMANZYXphysical
22939629
AL7A1_HUMANALDH7A1physical
22863883
CPNS1_HUMANCAPNS1physical
22863883
CNBP_HUMANCNBPphysical
22863883
DFFA_HUMANDFFAphysical
22863883
IF5_HUMANEIF5physical
22863883
ERP44_HUMANERP44physical
22863883
G3P_HUMANGAPDHphysical
22863883
HNRPK_HUMANHNRNPKphysical
22863883
GRP75_HUMANHSPA9physical
22863883
ISOC1_HUMANISOC1physical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
PDC10_HUMANPDCD10physical
22863883
SCLY_HUMANSCLYphysical
22863883
RUXF_HUMANSNRPFphysical
22863883
TBCB_HUMANTBCBphysical
22863883
UBFD1_HUMANUBFD1physical
22863883
XPO1_HUMANXPO1physical
22863883
1433E_HUMANYWHAEphysical
22863883
1433F_HUMANYWHAHphysical
22863883
1433Z_HUMANYWHAZphysical
22863883
ARBK1_HUMANADRBK1physical
26344197
ILK_HUMANILKphysical
26344197
MK01_HUMANMAPK1physical
26344197
MK03_HUMANMAPK3physical
26344197
NAA50_HUMANNAA50physical
26344197
PFKAM_HUMANPFKMphysical
26344197
PICAL_HUMANPICALMphysical
26344197
CKLF5_HUMANCMTM5physical
21516116
BIRC6_HUMANBIRC6physical
28514442
BBS12_HUMANBBS12physical
27173435
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 FERM2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASSSPECTROMETRY.
"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-159; SER-181 ANDSER-666, AND MASS SPECTROMETRY.
"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 SER-666, 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 SER-159, AND MASSSPECTROMETRY.

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