FMNL2_HUMAN - dbPTM
FMNL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMNL2_HUMAN
UniProt AC Q96PY5
Protein Name Formin-like protein 2
Gene Name FMNL2
Organism Homo sapiens (Human).
Sequence Length 1086
Subcellular Localization Cytoplasm.
Protein Description Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics..
Protein Sequence MGNAGSMDSQQTDFRAHNVPLKLPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQERFQVKNPPHTYIQKLKGYLDPAVTRKKFRRRVQESTQVLRELEISLRTNHIGWVREFLNEENKGLDVLVEYLSFAQYAVTFDFESVESTVESSVDKSKPWSRSIEDLHRGSNLPSPVGNSVSRSGRHSALRYNTLPSRRTLKNSRLVSKKDDVHVCIMCLRAIMNYQYGFNMVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILSAFDNFKEVCGEKQRFEKLMEHFRNEDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQKKGDGDIAILPVVASGTLSMGSEVVAGNSVGPTMGAASSGPLPPPPPPLPPSSDTPETVQNGPVTPPMPPPPPPPPPPPPPPPPPPPPPLPGPAAETVPAPPLAPPLPSAPPLPGTSSPTVVFNSGLAAVKIKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKIPQKGSNKVTLLEANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERKPLENLSDEDRFMMQFSKIERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHNTLLKEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQDPKSPSHKSKRQQQELIAELRRRQVKDNRHVYEGKDGAIEDIITVLKTVPFTARTAKRGSRFFCEPVLTEEYHY
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
2N-myristoyl glycine------MGNAGSMDS
------CCCCCCCCC		43.96-
2Myristoylation------MGNAGSMDS
------CCCCCCCCC		43.9620213681
9PhosphorylationGNAGSMDSQQTDFRA
CCCCCCCCCCCCCCC		18.6224247654
55 (in isoform 3)Phosphorylation-17.82-
55PhosphorylationKARLLRQYDNEKKWE
HHHHHHHHCCHHCEE		17.8220068231
60UbiquitinationRQYDNEKKWELICDQ
HHHCCHHCEEEEECC		39.4629967540
92PhosphorylationGYLDPAVTRKKFRRR
CCCCHHHHHHHHHHH		38.5925159151
92 (in isoform 3)Phosphorylation-38.5927251275
169PhosphorylationVDKSKPWSRSIEDLH
CCCCCCCCCCHHHHH		25.3629507054
171 (in isoform 3)Phosphorylation-25.4724719451
171PhosphorylationKSKPWSRSIEDLHRG
CCCCCCCCHHHHHCC		25.4729255136
179PhosphorylationIEDLHRGSNLPSPVG
HHHHHCCCCCCCCCC		34.8420068231
179 (in isoform 3)Phosphorylation-34.8421406692
183 (in isoform 3)Phosphorylation-35.0724719451
183PhosphorylationHRGSNLPSPVGNSVS
HCCCCCCCCCCCCCC		35.0726055452
188PhosphorylationLPSPVGNSVSRSGRH
CCCCCCCCCCCCCCC		18.6226055452
190PhosphorylationSPVGNSVSRSGRHSA
CCCCCCCCCCCCCCC		22.1328450419
200PhosphorylationGRHSALRYNTLPSRR
CCCCCHHCCCCCCCC		17.2223927012
202 (in isoform 3)Phosphorylation-30.9824719451
202PhosphorylationHSALRYNTLPSRRTL
CCCHHCCCCCCCCCC		30.9825884760
205PhosphorylationLRYNTLPSRRTLKNS
HHCCCCCCCCCCCCC		37.1923927012
212O-linked_GlycosylationSRRTLKNSRLVSKKD
CCCCCCCCCCCCCCC		25.9630379171
216PhosphorylationLKNSRLVSKKDDVHV
CCCCCCCCCCCCHHH		38.2828857561
234PhosphorylationCLRAIMNYQYGFNMV
HHHHHHHCCCCCCCC		5.9218083107
236PhosphorylationRAIMNYQYGFNMVMS
HHHHHCCCCCCCCCC		17.2118083107
352PhosphorylationTKLGLDEYLDKLKHT
HHCCHHHHHHHCCCC		21.62-
355UbiquitinationGLDEYLDKLKHTESD
CHHHHHHHCCCCCCC		57.7633845483
357UbiquitinationDEYLDKLKHTESDKL
HHHHHHCCCCCCCHH		54.9730230243
403PhosphorylationEELEENISHLSEKLQ
HHHHHHHHHHHHHHH		29.9221815630
406 (in isoform 3)Phosphorylation-27.5424719451
406PhosphorylationEENISHLSEKLQDTE
HHHHHHHHHHHHHHH		27.5429255136
412PhosphorylationLSEKLQDTENEAMSK
HHHHHHHHHHHHHHH		27.96-
418PhosphorylationDTENEAMSKIVELEK
HHHHHHHHHHHHHHH		26.69-
425UbiquitinationSKIVELEKQLMQRNK
HHHHHHHHHHHHHCH		62.4530230243
441PhosphorylationLDVVREIYKDANTQV
HHHHHHHHHHHHHHH		9.6928152594
446PhosphorylationEIYKDANTQVHTLRK
HHHHHHHHHHHHHHH		33.4223403867
450PhosphorylationDANTQVHTLRKMVKE
HHHHHHHHHHHHHHH		29.4229255136
453"N6,N6-dimethyllysine"TQVHTLRKMVKEKEE
HHHHHHHHHHHHHHH		51.67-
453MethylationTQVHTLRKMVKEKEE
HHHHHHHHHHHHHHH		51.6723644510
456"N6,N6-dimethyllysine"HTLRKMVKEKEEAIQ
HHHHHHHHHHHHHHH		60.62-
456MethylationHTLRKMVKEKEEAIQ
HHHHHHHHHHHHHHH		60.6223644510
458MethylationLRKMVKEKEEAIQRQ
HHHHHHHHHHHHHHH		55.9523644510
458"N6,N6-dimethyllysine"LRKMVKEKEEAIQRQ
HHHHHHHHHHHHHHH		55.95-
466PhosphorylationEEAIQRQSTLEKKIH
HHHHHHHHHHHHHHH		36.8329514088
467PhosphorylationEAIQRQSTLEKKIHE
HHHHHHHHHHHHHHH		30.5127273156
522PhosphorylationGPTMGAASSGPLPPP
CCCCCCCCCCCCCCC		34.98-
523PhosphorylationPTMGAASSGPLPPPP
CCCCCCCCCCCCCCC		39.44-
677PhosphorylationQGPAIDLSSSKQKIP
CCCCCCCCCCCCCCC		28.9025850435
677 (in isoform 3)Phosphorylation-28.9024719451
678PhosphorylationGPAIDLSSSKQKIPQ
CCCCCCCCCCCCCCC		49.1829743597
678 (in isoform 3)Phosphorylation-49.1827251275
679PhosphorylationPAIDLSSSKQKIPQK
CCCCCCCCCCCCCCC		35.4125159151
680UbiquitinationAIDLSSSKQKIPQKG
CCCCCCCCCCCCCCC		58.5233845483
700UbiquitinationLLEANRAKNLAITLR
EEHHHHHHHHHHHHH		49.62-
718UbiquitinationKTADEICKAIHVFDL
CCHHHHHHHHHHCCC		56.9129967540
727PhosphorylationIHVFDLKTLPVDFVE
HHHCCCCCCCCCHHH		43.52-
735GlutathionylationLPVDFVECLMRFLPT
CCCCHHHHHHHHCCC		2.8022555962
742PhosphorylationCLMRFLPTENEVKVL
HHHHHCCCCCHHHHH		54.3028152594
747UbiquitinationLPTENEVKVLRLYER
CCCCCHHHHHHHHHH		29.4030230243
763PhosphorylationRKPLENLSDEDRFMM
CCCCCCCCHHHHHHH		51.00-
767MethylationENLSDEDRFMMQFSK
CCCCHHHHHHHHHHH		21.22-
783PhosphorylationERLMQKMTIMAFIGN
HHHHHHHHHHHHHHH		18.0323403867
799PhosphorylationAESIQMLTPQLHAII
HHHHHHHHHHHHHHH		12.0223403867
809PhosphorylationLHAIIAASVSIKSSQ
HHHHHHHHCCCCCHH		13.8423403867
831PhosphorylationIILALGNYMNSSKRG
HHHHHHHHHCCCCCC		8.89-
834PhosphorylationALGNYMNSSKRGAVY
HHHHHHCCCCCCCCC		22.24-
835PhosphorylationLGNYMNSSKRGAVYG
HHHHHCCCCCCCCCE		22.74-
841PhosphorylationSSKRGAVYGFKLQSL
CCCCCCCCEEEHHHC		19.13-
854PhosphorylationSLDLLLDTKSTDRKQ
HCEEEECCCCCCHHH		27.19-
904UbiquitinationENVLLDVKELQRGMD
HHHHHCHHHHHHCCC		52.9930230243
913O-linked_GlycosylationLQRGMDLTKREYTMH
HHHCCCCCCCCCCCC		24.6430379171
918PhosphorylationDLTKREYTMHDHNTL
CCCCCCCCCCCHHHH		11.8628509920
957PhosphorylationAFDDVVKYFGENPKT
HHHHHHHHHCCCCCC		12.7622468782
963UbiquitinationKYFGENPKTTPPSVF
HHHCCCCCCCCCCHH		76.3030230243
968PhosphorylationNPKTTPPSVFFPVFV
CCCCCCCCHHHHHHH		32.5322468782
1016PhosphorylationMEQQDPKSPSHKSKR
HHCCCCCCCCHHHHH		36.7029255136
1016 (in isoform 3)Phosphorylation-36.7024719451
1017PhosphorylationEQQDPKSPSHKSKRQ
HCCCCCCCCHHHHHH		46.7217081983
1018 (in isoform 3)Phosphorylation-51.11-
1018PhosphorylationQQDPKSPSHKSKRQQ
CCCCCCCCHHHHHHH		51.1129255136
1044 (in isoform 3)Phosphorylation-16.9127642862
1047AcetylationNRHVYEGKDGAIEDI
CCCEECCCCCHHHHH		40.8420167786
1072 (in isoform 3)Phosphorylation-29.92-
1084PhosphorylationEPVLTEEYHY-----
CCCCCCCCCC-----		10.5327642862
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
1016SPhosphorylationKinaseCDK1P06493
PSP
1072SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FMNL2_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 FMNL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 FMNL2_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"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 SER-171, 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-171, 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 SER-1016, 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-1016, AND MASSSPECTROMETRY.

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