CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016088
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Filamin-B 
Protein Synonyms/Alias
 FLN-B; ABP-280-like protein; Actin-binding-like protein; Beta-filamin 
Gene Name
 Flnb 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
6**MPVTEKDLAEDAPacetylation[1]
313TPDSDKNKTYSVEYLacetylation[2]
349PFEVNVDKAQGDASKacetylation[2]
349PFEVNVDKAQGDASKsuccinylation[2]
492GELGVTVKGPKGLEEubiquitination[3]
495GVTVKGPKGLEELVKubiquitination[3]
502KGLEELVKQKGFLDGacetylation[2]
502KGLEELVKQKGFLDGsuccinylation[2]
502KGLEELVKQKGFLDGubiquitination[3]
551GPEAGMQKVRAWGPGacetylation[2]
551GPEAGMQKVRAWGPGsuccinylation[2]
607NDGSCDVKYWPKEPGacetylation[1]
681DAGSAPLKILAQDGEacetylation[4]
697QPIDIQMKSRMDGTYubiquitination[3]
838PASPFRVKVDPSHDAacetylation[2]
849SHDASKVKAEGPGLSacetylation[2]
849SHDASKVKAEGPGLSsuccinylation[2]
946AAPLDLSKIKINGLEacetylation[4]
987TILSPSRKVVPCLVAacetylation[1]
1232AIDTSGIKAFGPGIEacetylation[2]
1232AIDTSGIKAFGPGIEsuccinylation[2]
1241FGPGIEGKDVFREATacetylation[2]
1241FGPGIEGKDVFREATsuccinylation[2]
1241FGPGIEGKDVFREATubiquitination[3]
1339HAQGPGLKEAFTNKSubiquitination[3]
1345LKEAFTNKSNVFTVVacetylation[2]
1416SPFRVPSKDVVDPSKacetylation[2]
1416SPFRVPSKDVVDPSKsuccinylation[2]
1508EIPRSPFKVKVLPTYubiquitination[3]
1510PRSPFKVKVLPTYDAacetylation[2]
1510PRSPFKVKVLPTYDAsuccinylation[2]
1572RATVHDNKDGTYAVTacetylation[2]
1572RATVHDNKDGTYAVTsuccinylation[2]
1572RATVHDNKDGTYAVTubiquitination[3]
1641VGFVVDAKTAGKGKVubiquitination[3]
1780TPEIVDNKDGTVTVRacetylation[2]
1780TPEIVDNKDGTVTVRubiquitination[3]
1801GLHEMHIKYRGSHIPacetylation[2, 4]
1897ILVKYNDKHIPGSPFubiquitination[3]
2088PGSPFTVKISGEGRVacetylation[4]
2088PGSPFTVKISGEGRVubiquitination[3]
2170GVHTVSVKYRGQHVTacetylation[1, 2, 4]
2342VSELEPDKYAVRFIPacetylation[1, 2, 4]
2518DASKVTSKGAGLSKAacetylation[2]
2518DASKVTSKGAGLSKAsuccinylation[2]
2524SKGAGLSKAFVGQKSacetylation[2]
2524SKGAGLSKAFVGQKSsuccinylation[2]
2524SKGAGLSKAFVGQKSubiquitination[3]
2530SKAFVGQKSSFLVDCacetylation[2]
2566VSMKHVGKQQYNVTYacetylation[4]
2566VSMKHVGKQQYNVTYubiquitination[3]
2576YNVTYVVKERGDYVLacetylation[1, 4]
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] 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]
 [3] 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]
 [4] 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] 
Functional Description
 Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton (By similarity). 
Sequence Annotation
 DOMAIN 1 239 Actin-binding.
 DOMAIN 16 122 CH 1.
 DOMAIN 139 239 CH 2.
 REPEAT 249 347 Filamin 1.
 REPEAT 349 446 Filamin 2.
 REPEAT 447 543 Filamin 3.
 REPEAT 544 636 Filamin 4.
 REPEAT 640 736 Filamin 5.
 REPEAT 737 839 Filamin 6.
 REPEAT 840 938 Filamin 7.
 REPEAT 939 1034 Filamin 8.
 REPEAT 1035 1127 Filamin 9.
 REPEAT 1128 1222 Filamin 10.
 REPEAT 1223 1322 Filamin 11.
 REPEAT 1323 1415 Filamin 12.
 REPEAT 1416 1511 Filamin 13.
 REPEAT 1512 1608 Filamin 14.
 REPEAT 1609 1704 Filamin 15.
 REPEAT 1729 1813 Filamin 16.
 REPEAT 1816 1908 Filamin 17.
 REPEAT 1919 1994 Filamin 18.
 REPEAT 1997 2089 Filamin 19.
 REPEAT 2091 2185 Filamin 20.
 REPEAT 2188 2280 Filamin 21.
 REPEAT 2282 2375 Filamin 22.
 REPEAT 2379 2471 Filamin 23.
 REPEAT 2507 2601 Filamin 24.
 REGION 1705 1728 Hinge 1 (By similarity).
 REGION 2472 2602 Self-association site, tail (By
 REGION 2472 2506 Hinge 2 (By similarity).
 MOD_RES 519 519 Phosphothreonine (By similarity).
 MOD_RES 681 681 N6-acetyllysine (By similarity).
 MOD_RES 730 730 Phosphoserine (By similarity).
 MOD_RES 886 886 Phosphoserine (By similarity).
 MOD_RES 932 932 Phosphoserine (By similarity).
 MOD_RES 983 983 Phosphoserine (By similarity).
 MOD_RES 1028 1028 Phosphoserine (By similarity).
 MOD_RES 1316 1316 Phosphoserine (By similarity).
 MOD_RES 1433 1433 Phosphoserine (By similarity).
 MOD_RES 1505 1505 Phosphoserine (By similarity).
 MOD_RES 1557 1557 Phosphothreonine.
 MOD_RES 1602 1602 Phosphoserine (By similarity).
 MOD_RES 2083 2083 Phosphoserine (By similarity).
 MOD_RES 2369 2369 Phosphoserine (By similarity).
 MOD_RES 2465 2465 Phosphoserine (By similarity).
 MOD_RES 2478 2478 Phosphoserine (By similarity).
 MOD_RES 2481 2481 Phosphoserine (By similarity).
 MOD_RES 2576 2576 N6-acetyllysine (By similarity).
 CROSSLNK 2468 2468 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2602 AA 
Protein Sequence
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK 60
RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH 120
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP 180
GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA 240
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK 300
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK 360
GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP 420
VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK 480
AAGSGELGVT VKGPKGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE 540
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN 600
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC 660
TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV 720
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG 780
IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD 840
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID 900
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK 960
DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY 1020
DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP 1080
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG 1140
PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG 1200
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ 1260
VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV 1320
AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD 1380
GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP 1440
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE 1500
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE 1560
GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT 1620
GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK 1680
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN 1740
GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI 1800
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG 1860
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL 1920
GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK 1980
NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE 2040
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT 2100
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ 2160
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE 2220
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV 2280
IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP 2340
DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG 2400
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN 2460
HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA 2520
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD 2580
YVLAVKWGEE HIPGSPFHVT VP 2602 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; ISA:MGI.
 GO:0005925; C:focal adhesion; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0001725; C:stress fiber; IDA:MGI.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
 GO:0007519; P:skeletal muscle tissue development; 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