CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016583
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
87LLEVLSQKKMHRKHNubiquitination[1]
508ADFKVYTKGAGSGELubiquitination[1]
1071PTKPSKVKAFGPGLQubiquitination[1]
1294QTGGPHVKARVANPSubiquitination[1]
1477SFQVDTSKAGVAPLQubiquitination[1]
1491QVKVQGPKGLVEPVDubiquitination[1]
1824QPSITDNKDGTVTVRubiquitination[1]
Reference
 [1] 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] 
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 (By similarity). 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. 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 1641 1740 Filamin 15.
 REPEAT 1765 1860 Filamin 16.
 REPEAT 1861 1952 Filamin 17.
 REPEAT 1953 2039 Filamin 18.
 REPEAT 2042 2134 Filamin 19.
 REPEAT 2135 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.
 REGION 1741 1778 Hinge 1 (By similarity).
 REGION 2517 2647 Self-association site, tail (By
 REGION 2517 2553 Hinge 2 (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 11 11 Phosphoserine (By similarity).
 MOD_RES 508 508 N6-acetyllysine (By similarity).
 MOD_RES 700 700 N6-acetyllysine (By similarity).
 MOD_RES 781 781 N6-acetyllysine (By similarity).
 MOD_RES 837 837 N6-acetyllysine (By similarity).
 MOD_RES 1084 1084 Phosphoserine (By similarity).
 MOD_RES 1089 1089 Phosphothreonine (By similarity).
 MOD_RES 1286 1286 Phosphothreonine.
 MOD_RES 1338 1338 Phosphoserine (By similarity).
 MOD_RES 1459 1459 Phosphoserine.
 MOD_RES 1533 1533 Phosphoserine (By similarity).
 MOD_RES 1630 1630 Phosphoserine (By similarity).
 MOD_RES 1734 1734 Phosphoserine (By similarity).
 MOD_RES 1750 1750 Phosphothreonine.
 MOD_RES 2053 2053 Phosphoserine (By similarity).
 MOD_RES 2152 2152 Phosphoserine.
 MOD_RES 2158 2158 Phosphoserine (By similarity).
 MOD_RES 2284 2284 Phosphoserine (By similarity).
 MOD_RES 2327 2327 Phosphoserine (By similarity).
 MOD_RES 2336 2336 Phosphothreonine (By similarity).
 MOD_RES 2414 2414 Phosphoserine (By similarity).
 MOD_RES 2510 2510 Phosphoserine (By similarity).
 MOD_RES 2607 2607 N6-acetyllysine (By similarity).
 MOD_RES 2621 2621 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2647 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 DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG 1680
KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA 1740
LAGDQPTVQT PLRSQQLAPQ YNYPQGSQQT WIPERPMVGV NGLDVTSLRP FDLVIPFTIK 1800
KGEITGEVRM PSGKVAQPSI TDNKDGTVTV RYSPSEAGLH EMDIRYDNMH IPGSPLQFYV 1860
DYVNCGHITA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC 1920
SVSYLPVLPG DYSILVKYND QHIPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL 1980
SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS 2040
QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG 2100
TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANIGSHC 2160
DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGMH TVSVKYKGQH 2220
VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEVGVPAEFG IWTREAGAGG LAIAVEGPSK 2280
AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL 2340
QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGIY 2400
LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGSPAEF IVNTSNAGAG 2460
ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR 2520
LVSNHSLHET SSVFVDSLTK VATVPQHATS GPGPADVSKV VAKGLGLSKA YVGQKSNFTV 2580
DCSKAGNNML LVGVHGPRTP CEEILVKHMG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS 2640
PYRIMVP 2647 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0031523; C:Myb complex; ISO:MGI.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0005802; C:trans-Golgi network; IDA:MGI.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0034988; F:Fc-gamma receptor I complex binding; ISS:UniProtKB.
 GO:0001948; F:glycoprotein binding; ISS:UniProtKB.
 GO:0005080; F:protein kinase C binding; IDA:MGI.
 GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
 GO:0004871; F:signal transducer activity; ISS:UniProtKB.
 GO:0008134; F:transcription factor binding; ISS:UniProtKB.
 GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
 GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
 GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; ISS:UniProtKB.
 GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
 GO:0051220; P:cytoplasmic sequestering of protein; ISS:UniProtKB.
 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; ISS:UniProtKB.
 GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB.
 GO:0042993; P:positive regulation of transcription factor import into nucleus; ISS:UniProtKB.
 GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
 GO:0050821; P:protein stabilization; ISS:UniProtKB.
 GO:0043113; P:receptor clustering; ISS:UniProtKB.
 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