CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001163
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Filamin-B 
Protein Synonyms/Alias
 FLN-B; ABP-278; ABP-280 homolog; Actin-binding-like protein; Beta-filamin; Filamin homolog 1; Fh1; Filamin-3; Thyroid autoantigen; Truncated actin-binding protein; Truncated ABP 
Gene Name
 FLNB 
Gene Synonyms/Alias
 FLN1L; FLN3; TABP; TAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16AEDAPWKKIQQNTFTubiquitination[1]
60LLEVLSQKRMYRKYHubiquitination[2]
340FAGQHISKSPFEVSVubiquitination[3]
495GVTMKGPKGLEELVKubiquitination[3, 4]
681DAGKAPLKIFAQDGEacetylation[5]
681DAGKAPLKIFAQDGEubiquitination[4]
1241FGPGIEGKDVFREATubiquitination[3]
1449SFTVDSSKAGLAPLEubiquitination[3]
1757VIPFAVRKGEITGEVubiquitination[6]
1897ILVKYNDKHIPGSPFubiquitination[3, 4]
1955RDEPCLLKRLPNNHIubiquitination[3, 4]
2170GVHTVSVKYRGQHVTacetylation[5]
2170GVHTVSVKYRGQHVTubiquitination[3]
2316AIRLNGAKGKIDAKVubiquitination[1]
2576YNVTYVVKERGDYVLacetylation[5]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] 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]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
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. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro. 
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 1128 1511 Interaction with FBLP1.
 REGION 1705 1728 Hinge 1 (By similarity).
 REGION 1862 2148 Interaction with the cytoplasmic tail of
 REGION 2060 2225 Interaction with FLNA 1.
 REGION 2130 2602 Interaction with INPPL1.
 REGION 2472 2602 Self-association site, tail (By
 REGION 2472 2506 Hinge 2 (By similarity).
 REGION 2507 2602 Interaction with FLNA 2.
 MOD_RES 519 519 Phosphothreonine.
 MOD_RES 681 681 N6-acetyllysine.
 MOD_RES 730 730 Phosphoserine.
 MOD_RES 886 886 Phosphoserine.
 MOD_RES 932 932 Phosphoserine.
 MOD_RES 983 983 Phosphoserine.
 MOD_RES 1028 1028 Phosphoserine.
 MOD_RES 1316 1316 Phosphoserine.
 MOD_RES 1433 1433 Phosphoserine.
 MOD_RES 1505 1505 Phosphoserine.
 MOD_RES 1557 1557 Phosphothreonine (By similarity).
 MOD_RES 1602 1602 Phosphoserine.
 MOD_RES 2083 2083 Phosphoserine.
 MOD_RES 2107 2107 Phosphoserine.
 MOD_RES 2369 2369 Phosphoserine.
 MOD_RES 2465 2465 Phosphoserine.
 MOD_RES 2478 2478 Phosphoserine.
 MOD_RES 2481 2481 Phosphoserine.
 MOD_RES 2576 2576 N6-acetyllysine.
 CROSSLNK 2468 2468 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Disease mutation; Dwarfism; Isopeptide bond; Myogenesis; Phosphoprotein; Polymorphism; 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
RMYRKYHQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH 120
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP 180
GLCPDWESWD PQKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA 240
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK 300
EEAQVTPDSD KNKTYSVEYL PKVTGLHKVT VLFAGQHISK SPFEVSVDKA QGDASKVTAK 360
GPGLEAVGNI ANKPTYFDIY TAGAGVGDIG VEVEDPQGKN TVELLVEDKG NQVYRCVYKP 420
MQPGPHVVKI FFAGDTIPKS PFVVQVGEAC NPNACRASGR GLQPKGVRIR ETTDFKVDTK 480
AAGSGELGVT MKGPKGLEEL VKQKDFLDGV YAFEYYPSTP GRYSIAITWG GHHIPKSPFE 540
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG SLGFAIEGPS QAKIEYNDQN 600
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GGYNPDLVRA YGPGLEKSGC 660
IVNNLAEFTV DPKDAGKAPL KIFAQDGEGQ RIDIQMKNRM DGTYACSYTP VKAIKHTIAV 720
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG 780
IKCDARVLSE DEEDVDFDII HNANDTFTVK YVPPAAGRYT IKVLFASQEI PASPFRVKVD 840
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV YTKGAGKAPL NVQFNSPLPG DAVKDLDIID 900
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKLN GLENRVEVGK 960
DQEFTVDTRG AGGQGKLDVT ILSPSRKVVP CLVTPVTGRE NSTAKFIPRE EGLYAVDVTY 1020
DGHPVPGSPY TVEASLPPDP SKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP 1080
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG 1140
PGLEHGKVGE AGLLSVDCSE AGPGALGLEA VSDSGTKAEV SIQNNKDGTY AVTYVPLTAG 1200
MYTLTMKYGG ELVPHFPARV KVEPAVDTSR IKVFGPGIEG KDVFREATTD FTVDSRPLTQ 1260
VGGDHIKAHI ANPSGASTEC FVTDNADGTY QVEYTPFEKG LHVVEVTYDD VPIPNSPFKV 1320
AVTEGCQPSR VQAQGPGLKE AFTNKPNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD 1380
GSCSAEYIPF APGDYDVNIT YGGAHIPGSP FRVPVKDVVD PSKVKIAGPG LGSGVRARVL 1440
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YMVSVKYADE 1500
EIPRSPFKVK VLPTYDASKV TASGPGLSSY GVPASLPVDF AIDARDAGEG LLAVQITDQE 1560
GKPKRAIVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDDIP LSPYRIRATQ TGDASKCLAT 1620
GPGIASTVKT GEEVGFVVDA KTAGKGKVTC TVLTPDGTEA EADVIENEDG TYDIFYTAAK 1680
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AVEEAPVNAC PPGFRPWVTE EAYVPVSDMN 1740
GLGFKPFDLV IPFAVRKGEI TGEVHMPSGK TATPEIVDNK DGTVTVRYAP TEVGLHEMHI 1800
KYMGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG 1860
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DSRRCSQVKL 1920
GSAADFLLDI SETDLSSLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK 1980
NGNHVANSPV SIMVVQSEIG DARRAKVYGR GLSEGRTFEM SDFIVDTRDA GYGGISLAVE 2040
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVKESIT 2100
RTSRAPSVAT VGSICDLNLK IPEINSSDMS AHVTSPSGRV TEAEIVPMGK NSHCVRFVPQ 2160
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGV PAEFSIWTRE 2220
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPESPYLVPV 2280
IAPSDDARRL TVMSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP 2340
DKYAVRFIPH ENGVHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GTGLEGGTTG 2400
IQSEFFINTT RAGPGTLSVT IEGPSKVKMD CQETPEGYKV MYTPMAPGNY LISVKYGGPN 2460
HIVGSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKASS DASKVTSKGA 2520
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGNQQYN VTYVVKERGD 2580
YVLAVKWGEE HIPGSPFHVT VP 2602 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0001725; C:stress fiber; IEA:Compara.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0007016; P:cytoskeletal anchoring at plasma membrane; TAS:ProtInc.
 GO:0007519; P:skeletal muscle tissue development; IEA:Compara. 
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