CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004945
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Filamin-A 
Protein Synonyms/Alias
 FLN-A; Actin-binding protein 280; ABP-280; Alpha-filamin; Endothelial actin-binding protein; Filamin-1; Non-muscle filamin 
Gene Name
 FLNA 
Gene Synonyms/Alias
 FLN; FLN1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
87LLEVLSQKKMHRKHNubiquitination[1]
299EPTGNMVKKRAEFTVubiquitination[1]
684ARGPGLEKTGVAVNKubiquitination[1]
906AKAAGKGKLDVQFSGubiquitination[1]
916VQFSGLTKGDAVRDVubiquitination[1]
1246PVPNFPSKLQVEPAVubiquitination[1]
1477SFQVDTSKAGVAPLQubiquitination[1]
1491QVKVQGPKGLVEPVDubiquitination[1]
1816QPTITDNKDGTVTVRubiquitination[1]
1956SMRMSHLKVGSAADIubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface- localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. 
Sequence Annotation
 DOMAIN 2 274 Actin-binding.
 DOMAIN 43 149 CH 1.
 DOMAIN 166 266 CH 2.
 REPEAT 276 374 Filamin 1.
 REPEAT 376 474 Filamin 2.
 REPEAT 475 570 Filamin 3.
 REPEAT 571 663 Filamin 4.
 REPEAT 667 763 Filamin 5.
 REPEAT 764 866 Filamin 6.
 REPEAT 867 965 Filamin 7.
 REPEAT 966 1061 Filamin 8.
 REPEAT 1062 1154 Filamin 9.
 REPEAT 1155 1249 Filamin 10.
 REPEAT 1250 1349 Filamin 11.
 REPEAT 1350 1442 Filamin 12.
 REPEAT 1443 1539 Filamin 13.
 REPEAT 1540 1636 Filamin 14.
 REPEAT 1649 1740 Filamin 15.
 REPEAT 1779 1860 Filamin 16.
 REPEAT 1861 1950 Filamin 17.
 REPEAT 1951 2039 Filamin 18.
 REPEAT 2042 2131 Filamin 19.
 REPEAT 2132 2230 Filamin 20.
 REPEAT 2233 2325 Filamin 21.
 REPEAT 2327 2420 Filamin 22.
 REPEAT 2424 2516 Filamin 23.
 REPEAT 2552 2646 Filamin 24.
 REGION 1490 1607 Interaction with furin (By similarity).
 REGION 1741 1778 Hinge 1.
 REGION 2517 2647 Self-association site, tail.
 REGION 2517 2551 Hinge 2.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 508 508 N6-acetyllysine.
 MOD_RES 700 700 N6-acetyllysine.
 MOD_RES 781 781 N6-acetyllysine.
 MOD_RES 837 837 N6-acetyllysine.
 MOD_RES 1081 1081 Phosphoserine.
 MOD_RES 1084 1084 Phosphoserine.
 MOD_RES 1089 1089 Phosphothreonine.
 MOD_RES 1286 1286 Phosphothreonine (By similarity).
 MOD_RES 1338 1338 Phosphoserine.
 MOD_RES 1459 1459 Phosphoserine.
 MOD_RES 1533 1533 Phosphoserine.
 MOD_RES 1630 1630 Phosphoserine.
 MOD_RES 1734 1734 Phosphoserine.
 MOD_RES 2053 2053 Phosphoserine.
 MOD_RES 2152 2152 Phosphoserine.
 MOD_RES 2158 2158 Phosphoserine.
 MOD_RES 2284 2284 Phosphoserine.
 MOD_RES 2327 2327 Phosphoserine.
 MOD_RES 2336 2336 Phosphothreonine.
 MOD_RES 2414 2414 Phosphoserine.
 MOD_RES 2510 2510 Phosphoserine.
 MOD_RES 2607 2607 N6-acetyllysine.
 MOD_RES 2621 2621 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2647 AA 
Protein Sequence
MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV 60
SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK 120
LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL 180
PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ 240
VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK 300
RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF 360
AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGTGEVEVVI 420
QDPMGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP 480
SACRAVGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF 540
EYYPMVPGTY IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE 600
AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM 660
ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HGGKAPLRVQ VQDNEGCPVE 720
ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA 780
KTGLKAHEPT YFTVDCAEAG QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP 840
RGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK 900
AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT YGGDPIPKSP 960
FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG QGKVASKIVG PSGAAVPCKV 1020
EPGLGADNSV VRFLPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG 1080
SAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF 1140
ADTHIPGSPF KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE 1200
AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC 1260
YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTETYVQ DRGDGMYKVE 1320
YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET 1380
RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV 1440
PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV 1500
DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV 1560
PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVTGRYTILI 1620
KYGGDEIPFS PYRVRAVPTG DASKCTVTGA GIGPTIQIGE ETVITVDTKA AGKGKVTCTV 1680
CTPDGSEVDV DVVENEDGTF DIFYTAPQPG KYVICVRFGG EHVPNSPFQV TALAGDQPSV 1740
QPPLRSQQLA PQYTYAQGGQ QTWAPERPLV GVNGLDVTSL RPFDLVIPFT IKKGEITGEV 1800
RMPSGKVAQP TITDNKDGTV TVRYAPSEAG LHEMDIRYDN MHIPGSPLQF YVDYVNCGHV 1860
TAYGPGLTHG VVNKPATFTV NTKDAGEGGL SLAIEGPSKA EISCTDNQDG TCSVSYLPVL 1920
PGDYSILVKY NEQHVPGSPF TARVTGDDSM RMSHLKVGSA ADIPINISET DLSLLTATVV 1980
PPSGREEPCL LKRLRNGHVG ISFVPKETGE HLVHVKKNGQ HVASSPIPVV ISQSEIGDAS 2040
RVRVSGQGLH EGHTFEPAEF IIDTRDAGYG GLSLSIEGPS KVDINTEDLE DGTCRVTYCP 2100
TEPGNYIINI KFADQHVPGS PFSVKVTGEG RVKESITRRR RAPSVANVGS HCDLSLKIPE 2160
ISIQDMTAQV TSPSGKTHEA EIVEGENHTY CIRFVPAEMG THTVSVKYKG QHVPGSPFQF 2220
TVGPLGEGGA HKVRAGGPGL ERAEAGVPAE FSIWTREAGA GGLAIAVEGP SKAEISFEDR 2280
KDGSCGVAYV VQEPGDYEVS VKFNEEHIPD SPFVVPVASP SGDARRLTVS SLQESGLKVN 2340
QPASFAVSLN GAKGAIDAKV HSPSGALEEC YVTEIDQDKY AVRFIPRENG VYLIDVKFNG 2400
THIPGSPFKI RVGEPGHGGD PGLVSAYGAG LEGGVTGNPA EFVVNTSNAG AGALSVTIDG 2460
PSKVKMDCQE CPEGYRVTYT PMAPGSYLIS IKYGGPYHIG GSPFKAKVTG PRLVSNHSLH 2520
ETSSVFVDSL TKATCAPQHG APGPGPADAS KVVAKGLGLS KAYVGQKSSF TVDCSKAGNN 2580
MLLVGVHGPR TPCEEILVKH VGSRLYSVSY LLKDKGEYTL VVKWGDEHIP GSPYRVVVP 2639 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IC:BHF-UCL.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0031523; C:Myb complex; IDA:MGI.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0005802; C:trans-Golgi network; IEA:Compara.
 GO:0051015; F:actin filament binding; IDA:BHF-UCL.
 GO:0034988; F:Fc-gamma receptor I complex binding; IDA:BHF-UCL.
 GO:0001948; F:glycoprotein binding; IDA:BHF-UCL.
 GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
 GO:0048365; F:Rac GTPase binding; IDA:BHF-UCL.
 GO:0017160; F:Ral GTPase binding; IDA:BHF-UCL.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0051764; P:actin crosslink formation; IDA:BHF-UCL.
 GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL.
 GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IMP:BHF-UCL.
 GO:0034329; P:cell junction assembly; TAS:Reactome.
 GO:0042384; P:cilium assembly; IMP:UniProtKB.
 GO:0051220; P:cytoplasmic sequestering of protein; IMP:BHF-UCL.
 GO:0045022; P:early endosome to late endosome transport; IEA:Compara.
 GO:0001837; P:epithelial to mesenchymal transition; IEA:Compara.
 GO:0045184; P:establishment of protein localization; IDA:BHF-UCL.
 GO:0042177; P:negative regulation of protein catabolic process; IMP:BHF-UCL.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0042993; P:positive regulation of transcription factor import into nucleus; IMP:UniProtKB.
 GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL.
 GO:0050821; P:protein stabilization; IMP:BHF-UCL.
 GO:0043113; P:receptor clustering; IDA:BHF-UCL.
 GO:0090307; P:spindle assembly involved in mitosis; IDA: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