CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012304
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Filamin-C 
Protein Synonyms/Alias
 FLN-C; FLNc; ABP-280-like protein; ABP-L; Actin-binding-like protein; Filamin-2; Gamma-filamin 
Gene Name
 FLNC 
Gene Synonyms/Alias
 ABPL; FLN2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
113FLEREHIKLVSIDSKacetylation[1]
498VKEVADFKVFTKGAGubiquitination[2]
502ADFKVFTKGAGSGELubiquitination[2]
734RCSYVPTKPIKHTIIacetylation[1]
776VYGPGVEKTGLKANEacetylation[1, 3]
776VYGPGVEKTGLKANEubiquitination[2]
832DNDTFTVKYTPPGAGacetylation[1]
895THFTVLTKGAGKAKLubiquitination[2]
968APPLDLSKIKVQGLNacetylation[1]
1014SRRPIPCKLEPGGGAacetylation[1]
1014SRRPIPCKLEPGGGAubiquitination[2]
1073CAYGPGLKGGLVGTPubiquitination[2]
1299VLNPSGAKTDTYVTDacetylation[1]
1299VLNPSGAKTDTYVTDubiquitination[2]
1367LEGGLVNKANRFTVEacetylation[3]
1367LEGGLVNKANRFTVEubiquitination[2]
1438SPFRVPVKDVVDPGKacetylation[1]
1532PRSPFKIKVLPAHDAubiquitination[2]
1818RPNITDNKDGTITVRacetylation[1]
1831VRYAPTEKGLHQMGIacetylation[1]
1935IIVRFDDKHIPGSPFacetylation[1]
2030HVTNSPFKILVGPSEacetylation[1, 3]
2030HVTNSPFKILVGPSEubiquitination[2]
2127PGSPFTVKVTGEGRMubiquitination[2]
2291GPHTVAVKYRGQHVPacetylation[1]
2291GPHTVAVKYRGQHVPubiquitination[2]
2316LGEGGAHKVRAGGTGubiquitination[2, 4, 5]
2630SSYSSIPKFSSDASKacetylation[1]
2630SSYSSIPKFSSDASKubiquitination[2]
2653SQAFVGQKNSFTVDCubiquitination[2]
2685PCEEVYVKHMGNRVYacetylation[1, 3, 6]
2699YNVTYTVKEKGDYILacetylation[1, 3]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 
Functional 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. 
Sequence Annotation
 DOMAIN 1 259 Actin-binding.
 DOMAIN 36 142 CH 1.
 DOMAIN 159 259 CH 2.
 REPEAT 270 368 Filamin 1.
 REPEAT 370 468 Filamin 2.
 REPEAT 469 565 Filamin 3.
 REPEAT 566 658 Filamin 4.
 REPEAT 662 758 Filamin 5.
 REPEAT 759 861 Filamin 6.
 REPEAT 862 960 Filamin 7.
 REPEAT 961 1056 Filamin 8.
 REPEAT 1057 1149 Filamin 9.
 REPEAT 1150 1244 Filamin 10.
 REPEAT 1245 1344 Filamin 11.
 REPEAT 1345 1437 Filamin 12.
 REPEAT 1438 1533 Filamin 13.
 REPEAT 1534 1630 Filamin 14.
 REPEAT 1635 1734 Filamin 15.
 REPEAT 1759 1853 Filamin 16.
 REPEAT 1854 1946 Filamin 17.
 REPEAT 1947 2033 Filamin 18.
 REPEAT 2036 2128 Filamin 19.
 REPEAT 2244 2306 Filamin 20.
 REPEAT 2309 2401 Filamin 21.
 REPEAT 2403 2496 Filamin 22.
 REPEAT 2500 2592 Filamin 23.
 REPEAT 2630 2724 Filamin 24.
 REGION 1735 1758 Hinge 1.
 REGION 2162 2243 Intradomain insert.
 REGION 2403 2724 Interaction with INPPL1.
 REGION 2593 2725 Self-association site, tail (By
 REGION 2593 2629 Hinge 2.
 MOD_RES 1161 1161 Phosphoserine.
 MOD_RES 2233 2233 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Membrane; Myofibrillar myopathy; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2725 AA 
Protein Sequence
MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVGKRLTDL 60
QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV SVALEFLERE HIKLVSIDSK 120
AIVDGNLKLI LGLIWTLILH YSISMPMWED EDDEDARKQT PKQRLLGWIQ NKVPQLPITN 180
FNRDWQDGKA LGALVDNCAP GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI 240
VDPNVDEHSV MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV 300
QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV TVLFAGQNIE 360
RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI YTAGAGTGDV AVVIVDPQGR 420
RDTVEVALED KGDSTFRCTY RPAMEGPHTV HVAFAGAPIT RSPFPVHVSE ACNPNACRAS 480
GRGLQPKGVR VKEVADFKVF TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV 540
VPGKYVVTIT WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE 600
VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR DSPFIAHILP 660
APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG DLKLYAQDAD GCPIDIKVIP 720
NGDGTFRCSY VPTKPIKHTI IISWGGVNVP KSPFRVNVGE GSHPERVKVY GPGVEKTGLK 780
ANEPTYFTVD CSEAGQGDVS IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR 840
YTIMVLFANQ EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA 900
KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP VPKSPFVVNV 960
APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD VRMTSPSRRP IPCKLEPGGG 1020
AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP 1080
APFSIDTKGA GTGGLGLTVE GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI 1140
PGSPFKATIR PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA 1200
EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT SGVKVSGPGV 1260
EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT DTYVTDNGDG TYRVQYTAYE 1320
EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP TRVRAFGPGL EGGLVNKANR FTVETRGAGT 1380
GGLGLAIEGP SEAKMSCKDN KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV 1440
VDPGKVKCSG PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT 1500
HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN ASGIPASLPV 1560
EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV SYLPDMSGRY TITIKYGGDE 1620
IPYSPFRIHA LPTGDASKCL VTVSIGGHGL GACLGPRIQI GQETVITVDA KAAGEGKVTC 1680
TVSTPDGAEL DVDVVENHDG TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLACDPLPH 1740
EEEPSEVPQL RQPYAPPRPG ARPTHWATEE PVVPVEPMES MLRPFNLVIP FAVQKGELTG 1800
EVRMPSGKTA RPNITDNKDG TITVRYAPTE KGLHQMGIKY DGNHIPGSPL QFYVDAINSR 1860
HVSAYGPGLS HGMVNKPATF TIVTKDAGEG GLSLAVEGPS KAEITCKDNK DGTCTVSYLP 1920
TAPGDYSIIV RFDDKHIPGS PFTAKITGDD SMRTSQLNVG TSTDVSLKIT ESDLSQLTAS 1980
IRAPSGNEEP CLLKRLPNRH IGISFTPKEV GEHVVSVRKS GKHVTNSPFK ILVGPSEIGD 2040
ASKVRVWGKG LSEGHTFQVA EFIVDTRNAG YGGLGLSIEG PSKVDINCED MEDGTCKVTY 2100
CPTEPGTYII NIKFADKHVP GSPFTVKVTG EGRMKESITR RRQAPSIATI GSTCDLNLKI 2160
PGNWFQMVSA QERLTRTFTR SSHTYTRTER TEISKTRGGE TKREVRVEES TQVGGDPFPA 2220
VFGDFLGRER LGSFGSITRQ QEGEASSQDM TAQVTSPSGK VEAAEIVEGE DSAYSVRFVP 2280
QEMGPHTVAV KYRGQHVPGS PFQFTVGPLG EGGAHKVRAG GTGLERGVAG VPAEFSIWTR 2340
EAGAGGLSIA VEGPSKAEIA FEDRKDGSCG VSYVVQEPGD YEVSIKFNDE HIPDSPFVVP 2400
VASLSDDARR LTVTSLQETG LKVNQPASFA VQLNGARGVI DARVHTPSGA VEECYVSELD 2460
SDKHTIRFIP HENGVHSIDV KFNGAHIPGS PFKIRVGEQS QAGDPGLVSA YGPGLEGGTT 2520
GVSSEFIVNT LNAGSGALSV TIDGPSKVQL DCRECPEGHV VTYTPMAPGN YLIAIKYGGP 2580
QHIVGSPFKA KVTGPRLSGG HSLHETSTVL VETVTKSSSS RGSSYSSIPK FSSDASKVVT 2640
RGPGLSQAFV GQKNSFTVDC SKAGTNMMMV GVHGPKTPCE EVYVKHMGNR VYNVTYTVKE 2700
KGDYILIVKW GDESVPGSPF KVKVP 2725 
Gene Ontology
 GO:0043034; C:costamere; TAS:BHF-UCL.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0042383; C:sarcolemma; IDA:BHF-UCL.
 GO:0016528; C:sarcoplasm; IEA:Compara.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
 GO:0034329; P:cell junction assembly; TAS:Reactome.
 GO:0048747; P:muscle fiber development; IEA:Compara. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR003961; Fibronectin_type3.
 IPR001298; Filamin.
 IPR017868; Filamin/ABP280_repeat-like.
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set. 
Pfam
 PF00307; CH
 PF00630; Filamin 
SMART
 SM00033; CH
 SM00060; FN3
 SM00557; IG_FLMN 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS50194; FILAMIN_REPEAT 
PRINTS