CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031875
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Filamin, alpha 
Protein Synonyms/Alias
 Filamin-A 
Gene Name
 Flna 
Gene Synonyms/Alias
 RP23-436K3.1-002 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
33AEMPATEKDLAEDAPacetylation[1]
42LAEDAPWKKIQQNTFacetylation[2]
43AEDAPWKKIQQNTFTacetylation[3]
43AEDAPWKKIQQNTFTsuccinylation[3]
43AEDAPWKKIQQNTFTubiquitination[4]
87LLEVLSQKKMHRKHNubiquitination[4]
127KLVSIDSKAIVDGNLacetylation[2]
270QFPKAKLKPGAPLRPacetylation[3]
270QFPKAKLKPGAPLRPsuccinylation[3]
299EPTGNMVKKRAEFTVacetylation[1, 2]
338KVTANNDKNRTFSVWacetylation[3]
367FAGQHIAKSPFEVYVacetylation[1, 2]
376PFEVYVDKSQGDASKacetylation[3]
376PFEVYVDKSQGDASKsuccinylation[3]
504VKETADFKVYTKGAGacetylation[1, 2]
508ADFKVYTKGAGSGELacetylation[1, 3]
508ADFKVYTKGAGSGELsuccinylation[3]
508ADFKVYTKGAGSGELubiquitination[4]
520GELKVTVKGPKGEERacetylation[3]
520GELKVTVKGPKGEERsuccinylation[3]
569GRSPFEVKVGTECGNacetylation[1, 2, 3]
626AKIECDDKGDGSCDVacetylation[1, 3]
684ARGPGLEKTGVAVNKacetylation[3]
684ARGPGLEKTGVAVNKsuccinylation[3]
691KTGVAVNKPAEFTVDacetylation[3, 5]
691KTGVAVNKPAEFTVDsuccinylation[3]
700AEFTVDAKHAGKAPLacetylation[1, 2, 3]
771GAGSHPNKVKVYGPGacetylation[3]
771GAGSHPNKVKVYGPGsuccinylation[3]
781VYGPGVAKTGLKAHEacetylation[1, 3]
865PTSPIRVKVEPSHDAacetylation[3]
874EPSHDASKVKAEGPGacetylation[3]
874EPSHDASKVKAEGPGsuccinylation[3]
876SHDASKVKAEGPGLNacetylation[3]
876SHDASKVKAEGPGLNsuccinylation[3]
891RTGVELGKPTHFTVNacetylation[2, 3]
906AKTAGKGKLDVQFSGacetylation[1, 2, 3]
906AKTAGKGKLDVQFSGsuccinylation[3]
936HDNTYTVKYIPVQQGacetylation[2]
958YGGDHIPKSPFSVGVacetylation[2]
973SPSLDLSKIKVSGLGacetylation[3]
973SPSLDLSKIKVSGLGsuccinylation[3]
987GDKVDVGKDQEFTVKacetylation[2, 3]
987GDKVDVGKDQEFTVKsuccinylation[3]
994KDQEFTVKSKGAGGQacetylation[3]
994KDQEFTVKSKGAGGQsuccinylation[3]
1007GQGKVASKIVSPSGAacetylation[3]
1007GQGKVASKIVSPSGAsuccinylation[3]
1019SGAAVPCKVEPGLGAacetylation[1, 2]
1071PTKPSKVKAFGPGLQacetylation[1, 3]
1071PTKPSKVKAFGPGLQsuccinylation[3]
1071PTKPSKVKAFGPGLQubiquitination[4]
1162APCFDASKVKCSGPGacetylation[2]
1294QTGGPHVKARVANPSacetylation[1, 3]
1294QTGGPHVKARVANPSsuccinylation[3]
1294QTGGPHVKARVANPSubiquitination[4]
1372IQSGTTNKPNKFTVEacetylation[3]
1450HDVTDASKVKCSGPGacetylation[3]
1450HDVTDASKVKCSGPGsuccinylation[3]
1452VTDASKVKCSGPGLSacetylation[3]
1452VTDASKVKCSGPGLSsuccinylation[3]
1477SFQVDTSKAGVAPLQacetylation[2]
1477SFQVDTSKAGVAPLQubiquitination[4]
1491QVKVQGPKGLVEPVDacetylation[2, 3]
1491QVKVQGPKGLVEPVDubiquitination[4]
1538PRSPFKVKVLPTHDAacetylation[3]
1547LPTHDASKVKASGPGacetylation[3]
1806EVRMPSGKVAQPSITacetylation[3]
1806EVRMPSGKVAQPSITsuccinylation[3]
1816QPSITDNKDGTVTVRacetylation[2, 3]
1816QPSITDNKDGTVTVRubiquitination[4]
1992REEPCLLKRLRNGHVacetylation[1]
2016GEHLVHVKKNGQHVAacetylation[1]
2125PGSPFSVKVTGEGRVacetylation[2]
2209HTVSVKYKGQHVPGSacetylation[3]
2281EISFEDRKDGSCGVAacetylation[2]
2379VTEIDQDKYAVRFIPacetylation[1]
2465IDGPSKVKMDCQECPacetylation[1, 3]
2465IDGPSKVKMDCQECPsuccinylation[3]
2551PGPADVSKVVAKGLGacetylation[1, 2, 3]
2551PGPADVSKVVAKGLGsuccinylation[3]
2555DVSKVVAKGLGLSKAacetylation[3]
2555DVSKVVAKGLGLSKAsuccinylation[3]
2561AKGLGLSKAYVGQKSacetylation[1, 2, 3]
2561AKGLGLSKAYVGQKSsuccinylation[3]
2567SKAYVGQKSNFTVDCacetylation[1, 3]
2599PCEEILVKHMGSRLYacetylation[1, 2, 3]
2599PCEEILVKHMGSRLYsuccinylation[3]
2613YSVSYLLKDKGEYTLacetylation[1, 2, 3]
2615VSYLLKDKGEYTLVVacetylation[1, 3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
  
Sequence Annotation
  
Keyword
 Actin-binding; Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2639 AA 
Protein Sequence
MSSSHSRCGQ SAAVASPGGS IDSRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV 60
SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK 120
LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL 180
PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVNNAREAMQ QADDWLGIPQ 240
VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK 300
RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF 360
AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGMGEVEVVI 420
QDPTGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP 480
AACRAIGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF 540
EYYPTIPGTY TVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGI VGKSADFVVE 600
AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM 660
ADIREAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HAGKAPLRVQ VQDNEGCSVE 720
ATVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA 780
KTGLKAHEPT YFTVDCTEAG QGDVSIGIKC APGVVGPTEA DIDFDIIRND NDTFTVKYTP 840
CGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLNRTGVELG KPTHFTVNAK 900
TAGKGKLDVQ FSGLAKGDAV RDVDIIDHHD NTYTVKYIPV QQGPVGVNVT YGGDHIPKSP 960
FSVGVSPSLD LSKIKVSGLG DKVDVGKDQE FTVKSKGAGG QGKVASKIVS PSGAAVPCKV 1020
EPGLGADNSV VRFVPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG 1080
NAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF 1140
ADTHIPGSPF KAHVAPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE 1200
AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC 1260
YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTDTYVQ DCGDGTYKVE 1320
YTPYEEGVHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET 1380
RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV 1440
PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV 1500
DNADGTQTVN YVPSREGSYS ISVLYGEEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV 1560
PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVPGRYTILI 1620
KYGGDEIPFS PYRVRAVPTG DASKCTVTGA GIGPTIQIGE ETVITVDTKA AGKGKVTCTV 1680
CTPDGSEVDV DVVENEDGTF DIFYTAPQPG KYVICVRFGG EHVPNSPFQV TALAGDQPTV 1740
QTPLRSQQLA PQYNYPQGSQ QTWIPERPMV GVNGLDVTSL RPFDLVIPFT IKKGEITGEV 1800
RMPSGKVAQP SITDNKDGTV TVRYSPSEAG LHEMDIRYDN MHIPGSPLQF YVDYVNCGHI 1860
TAYGPGLTHG VVNKPATFTV NTKDAGEGGL SLAIEGPSKA EISCTDNQDG TCSVSYLPVL 1920
PGDYSILVKY NDQHIPGSPF TARVTGDDSM RMSHLKVGSA ADIPINISET DLSLLTATVV 1980
PPSGREEPCL LKRLRNGHVG ISFVPKETGE HLVHVKKNGQ HVASSPIPVV ISQSEIGDAS 2040
RVRVSGQGLH EGHTFEPAEF IIDTRDAGYG GLSLSIEGPS KVDINTEDLE DGTCRVTYCP 2100
TEPGNYIINI KFADQHVPGS PFSVKVTGEG RVKESITRRR RAPSVANIGS HCDLSLKIPE 2160
ISIQDMTAQV TSPSGKTHEA EIVEGENHTY CIRFVPAEMG MHTVSVKYKG QHVPGSPFQF 2220
TVGPLGEGGA HKVRAGGPGL ERAEVGVPAE FGIWTREAGA GGLAIAVEGP SKAEISFEDR 2280
KDGSCGVAYV VQEPGDYEVS VKFNEEHIPD SPFVVPVASP SGDARRLTVS SLQESGLKVN 2340
QPASFAVSLN GAKGAIDAKV HSPSGALEEC YVTEIDQDKY AVRFIPRENG IYLIDVKFNG 2400
THIPGSPFKI RVGEPGHGGD PGLVSAYGAG LEGGVTGSPA EFIVNTSNAG AGALSVTIDG 2460
PSKVKMDCQE CPEGYRVTYT PMAPGSYLIS IKYGGPYHIG GSPFKAKVTG PRLVSNHSLH 2520
ETSSVFVDSL TKVATVPQHA TSGPGPADVS KVVAKGLGLS KAYVGQKSNF TVDCSKAGNN 2580
MLLVGVHGPR TPCEEILVKH MGSRLYSVSY LLKDKGEYTL VVKWGDEHIP GSPYRIMVP 2639 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0031523; C:Myb complex; ISO:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005802; C:trans-Golgi network; IDA:MGI.
 GO:0003779; F:actin binding; TAS:MGI.
 GO:0005080; F:protein kinase C binding; IDA:MGI.
 GO:0004871; F:signal transducer activity; IEA:Compara.
 GO:0051764; P:actin crosslink formation; IEA:Compara.
 GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
 GO:0031532; P:actin cytoskeleton reorganization; IEA:Compara.
 GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:Compara.
 GO:0042384; P:cilium assembly; IEA:Compara.
 GO:0051220; P:cytoplasmic sequestering of protein; IEA:Compara.
 GO:0045022; P:early endosome to late endosome transport; IDA:MGI.
 GO:0001837; P:epithelial to mesenchymal transition; IGI:MGI.
 GO:0045184; P:establishment of protein localization; IEA:Compara.
 GO:0042177; P:negative regulation of protein catabolic process; IEA:Compara.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0042993; P:positive regulation of transcription factor import into nucleus; IEA:Compara.
 GO:0034394; P:protein localization to cell surface; IEA:Compara.
 GO:0050821; P:protein stabilization; IEA:Compara.
 GO:0043113; P:receptor clustering; IEA:Compara.
 GO:0090307; P:spindle assembly involved in mitosis; ISO:MGI. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR001298; Filamin.
 IPR017868; Filamin/ABP280_repeat-like.
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set. 
Pfam
 PF00307; CH
 PF00630; Filamin 
SMART
 SM00033; CH
 SM00557; IG_FLMN 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS50194; FILAMIN_REPEAT 
PRINTS