FLNC_RAT - dbPTM
FLNC_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLNC_RAT
UniProt AC D3ZHA0
Protein Name Filamin-C
Gene Name Flnc
Organism Rattus norvegicus (Rat).
Sequence Length 2726
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fra
Protein Description Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers..
Protein Sequence MMNNSNYSDASGLGLLDEADEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPVRSKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDKDRTYAVSYVPKVAGLHKVTVLFAGQNIERSPFEVNVGMALGDANKVSARGPGLEPVGNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRDTVEVALEDKGDNTFRCTYRPVMEGPHTVHVAFAGAPITRSPFPVHVAEACNPNACRASGRGLQPKGVRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVIPGKYVVTITWGGYAIPRSPFEVQVSPEAGAQKVRAWGPGLETGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECDDRGDGSCDVRYWPTEPGEYAVHVICDDEDIRDSPFIAHIQPAPPDCFPDKVKAFGPGLEPTGCIVDRPAEFTIDARAAGKGDLKLYAQDADGCPIDIKVIPNGDGTFRCSYVPTKPIKHTVIISWGGVNVPKSPFRVNVGEGSHPERVKVYGPGVEKTGLKANEPTYFTVDCSEAGQGDVSIGIKCAPGVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGHYTIMVLFANQEIPASPFHIKVDPSHDASKVKAEGPGLSRTGVEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAVRDFEIIDNHDYSYTVKYTAVQQGNMAVTVTYGGDPVPKSPFVVNVAPPLDLSKVKVQGLNSKVAVGEEQAFLVNTRGAGGQGQLDVRMTSPSRRPIPCKLEPGSGAEAQAVRYMPPEEGPYKVDITYDGHPVPGSPFAVEGVLPPDPSKVCAYGPGLKGGLVGTPAPFSIDTKGAGTGGLGLTVEGPCEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAHIPGSPFKATIQPVFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHPIPKFPTRVHVQPAVDTSGIKVSGPGVEPHGVLREVTTEFTVDARSLTATGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLYDEVAVPKSPFRVGVTEGCDPTRVRAFGPGLEGGLVNKANRFTVETRGAGTGGLGLAIEGPSEAKMSCKDNKDGSCTVEYVPFTPGDYDVNITFGGQPIPGSPFRVPVKDVVDPGKVKCSGPGLGTGVRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVRDNGDGTHTVHYTPATDGPYTVAVKYADQEVPRSPFKIKVLPAHDASKVRASGPGLNASGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGGDEIPYSPFRIHALPTGDASKCLVTVSIGGHGLGACLGPRIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVLACDPLPHVEEPAEVLQLHQPYAPLRPGTCPTHWATEEPVVPVEPLESMLRPFNLVIPFTVQKGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVDAINSGHVSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPSKAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPGSPFTAKITGDDSMRTSQLNVGTSTDVSLKITEGDLSQLTASIRAPSGNEEPCLLKRLPNRHIGISFTPKEVGEHVVSVRKSGKHVTNSPFKILVGPSEIGDASKVRVWGKGLSEGQTFQVAEFIVDTRNAGYGGLGLSIEGPSKVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKHVPGSPFTVKVTGEGRMKESITRRRQAPSIATIGSTCDLNLKIPGNWFQMVSAQERLTRTFTRSSHTYTRTERTEISKTRGGETKREVRVEESTQVGGDPFPAVFGDFLGRERLGSFGSITRQQEGEASSQDMTAQVTSPSGKTEAAEIVEGEDSAYSVRFVPQEMGPHTVAVKYRGQHVPGSPFQFTVGPLGEGGAHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEHIPDSPFVVPVASLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRVGEQSQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTQNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKVTGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNVP
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
5Phosphorylation---MMNNSNYSDASG
---CCCCCCCCCCCC
-
36AcetylationLAEDAPWKKIQQNTF
HHHCCCHHHHHHHHH
7668577
42PhosphorylationWKKIQQNTFTRWCNE
HHHHHHHHHHHHHHH
23984901
59PhosphorylationKCVGKRLTDLQRDLS
HHHHHHHHHHHHHHH
30181290
511AcetylationGAGSGELKVTVKGPK
CCCCCEEEEEEECCC
-
735AcetylationRCSYVPTKPIKHTVI
EEEECCCCCCCEEEE
26302492
738AcetylationYVPTKPIKHTVIISW
ECCCCCCCEEEEEEE
26302492
1003MethylationGQGQLDVRMTSPSRR
CCCCEEEEECCCCCC
-
1015AcetylationSRRPIPCKLEPGSGA
CCCCCCCCCCCCCCC
66734001
1020PhosphorylationPCKLEPGSGAEAQAV
CCCCCCCCCCCEEEE
27097102
1162PhosphorylationDPSKVRASGPGLERG
CHHHCCCCCCCCCCC
-
1301PhosphorylationLNPSGAKTDTYVTDN
ECCCCCCCCEEEEEC
28826663
1303PhosphorylationPSGAKTDTYVTDNGD
CCCCCCCEEEEECCC
28826663
1304PhosphorylationSGAKTDTYVTDNGDG
CCCCCCEEEEECCCC
28826663
1306PhosphorylationAKTDTYVTDNGDGTY
CCCCEEEEECCCCEE
28826663
1312PhosphorylationVTDNGDGTYRVQYTA
EEECCCCEEEEEEEE
28826663
1313PhosphorylationTDNGDGTYRVQYTAY
EECCCCEEEEEEEEE
28826663
1331PhosphorylationVHLVEVLYDEVAVPK
EEEEEEEECCCCCCC
22673903
1339PhosphorylationDEVAVPKSPFRVGVT
CCCCCCCCCCCEECC
22673903
1531AcetylationEVPRSPFKIKVLPAH
CCCCCCCEEEEEECC
72616751
1936AcetylationIIVRFDDKHIPGSPF
EEEEECCCCCCCCCE
72610001
2043PhosphorylationPSEIGDASKVRVWGK
HHHCCCHHHEEEEEC
-
2234PhosphorylationLGRERLGSFGSITRQ
HCCCCCCCCCCCCCC
29779826
2237PhosphorylationERLGSFGSITRQQEG
CCCCCCCCCCCCCCC
27097102
2239PhosphorylationLGSFGSITRQQEGEA
CCCCCCCCCCCCCCC
27097102
2413PhosphorylationSDDARRLTVTSLQET
CHHHHHEEEEEHHHH
17564427
2464AcetylationVSELDSDKHTIRFIP
EEECCCCCCEEEEEE
26302492
2587PhosphorylationGPQHIVGSPFKAKVT
CCCCEECCCCCCEEC
-
2618PhosphorylationLVETVTKSSSSRGAS
EEEEECCCCCCCCCC
-
2621PhosphorylationTVTKSSSSRGASYSS
EECCCCCCCCCCCCC
-
2625PhosphorylationSSSSRGASYSSIPKF
CCCCCCCCCCCCCCC
27097102
2627PhosphorylationSSRGASYSSIPKFSS
CCCCCCCCCCCCCCC
27097102
2628PhosphorylationSRGASYSSIPKFSSD
CCCCCCCCCCCCCCC
27097102
2633PhosphorylationYSSIPKFSSDASKVV
CCCCCCCCCCCHHEE
-
2656PhosphorylationAFVGQKNSFTVDCSK
HHCCCCCEEEEECHH
27097102
2715PhosphorylationIVKWGDESVPGSPFK
EEEECCCCCCCCCCE
-
2719PhosphorylationGDESVPGSPFKVNVP
CCCCCCCCCCEECCC
-

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
2413TPhosphorylationKinasePRKACAP00517
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLNC_RAT !!

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 FLNC_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FLNC_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLNC_RAT

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Related Literatures of Post-Translational Modification

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