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Filamin-B (FLN-B) (ABP-280-like protein) (Actin-binding-like protein) (Beta-filamin)

 FLNB_MOUSE              Reviewed;        2602 AA.
Q80X90; E9QNV9; Q8VHX4; Q8VHX7; Q99KY3;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
23-MAY-2018, entry version 145.
RecName: Full=Filamin-B;
Short=FLN-B;
AltName: Full=ABP-280-like protein;
AltName: Full=Actin-binding-like protein;
AltName: Full=Beta-filamin;
Name=Flnb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1663-1752 AND 2031-2181.
STRAIN=C3H/HeJ;
PubMed=11807098; DOI=10.1083/jcb.200103037;
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
Takafuta T., Shapiro S.S., Sonnenberg A.;
"Different splice variants of filamin-B affect myogenesis, subcellular
distribution, and determine binding to integrin (beta) subunits.";
J. Cell Biol. 156:361-376(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1884-2602.
STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
"Filamin A and filamin B are co-expressed within neurons during
periods of neuronal migration and can physically interact.";
Hum. Mol. Genet. 11:2845-2854(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH RFLNA AND RFLNB.
PubMed=21709252; DOI=10.1073/pnas.1104211108;
Gay O., Gilquin B., Nakamura F., Jenkins Z.A., McCartney R.,
Krakow D., Deshiere A., Assard N., Hartwig J.H., Robertson S.P.,
Baudier J.;
"RefilinB (FAM101B) targets filamin A to organize perinuclear actin
networks and regulates nuclear shape.";
Proc. Natl. Acad. Sci. U.S.A. 108:11464-11469(2011).
[8]
INTERACTION WITH MICALL2.
PubMed=23890175; DOI=10.1111/gtc.12078;
Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K.,
Kitamura T., Imoto I., Matsushita N., Sasaki T.;
"Junctional Rab13-binding protein (JRAB) regulates cell spreading via
filamins.";
Genes Cells 18:810-822(2013).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1780, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-2518 AND LYS-2524, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
INTERACTION WITH RFLNA AND RFLNB.
PubMed=24436304; DOI=10.1093/hmg/ddu007;
Mizuhashi K., Kanamoto T., Moriishi T., Muranishi Y., Miyazaki T.,
Terada K., Omori Y., Ito M., Komori T., Furukawa T.;
"Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the
formation of cartilaginous skeletal elements.";
Hum. Mol. Genet. 23:2953-2967(2014).
-!- FUNCTION: 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). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A,
ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By
similarity). Interacts with MICALL2. Interacts with RFLNA and
RFLNB (PubMed:21709252,PubMed:24436304). {ECO:0000250,
ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm,
myofibril, sarcomere, Z line {ECO:0000250}. Cytoplasm,
cytoskeleton. Note=May localize also at actin stress fibers and
within the Z-lines. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in hippocampus, cortex, cerebellar
Purkinje cells and granule cell layers.
{ECO:0000269|PubMed:12393796}.
-!- DEVELOPMENTAL STAGE: Expressed within the ventricular,
periventricular and subventricular zones at 12.5 dpc; olfactory
epithelium, radial glial fibers, cortical plate and lateral
ventricles at 16 dpc; in a lesser degree in lung, renal cortices
and alimentary tract. {ECO:0000269|PubMed:12393796}.
-!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24
internally homologous repeats and two hinge regions. Repeat 24 and
the second hinge domain are important for dimer formation. The
first hinge region prevents binding to ITGA and ITGB subunits (By
similarity). {ECO:0000250}.
-!- PTM: ISGylation prevents ability to interact with the upstream
activators of the JNK cascade and inhibits IFNA-induced JNK
signaling. {ECO:0000250}.
-!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform
2 leads to proteasomal degradation which promotes muscle
differentiation. {ECO:0000250|UniProtKB:O75369}.
-!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC129222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF353669; AAL68445.1; -; mRNA.
EMBL; AF353672; AAL68448.1; -; mRNA.
EMBL; BC003959; AAH03959.1; -; mRNA.
EMBL; BC048835; AAH48835.1; -; mRNA.
CCDS; CCDS70540.1; -.
RefSeq; NP_001074896.1; NM_001081427.1.
UniGene; Mm.489652; -.
ProteinModelPortal; Q80X90; -.
SMR; Q80X90; -.
BioGrid; 235046; 106.
IntAct; Q80X90; 108.
MINT; Q80X90; -.
STRING; 10090.ENSMUSP00000052020; -.
iPTMnet; Q80X90; -.
PhosphoSitePlus; Q80X90; -.
SwissPalm; Q80X90; -.
EPD; Q80X90; -.
MaxQB; Q80X90; -.
PaxDb; Q80X90; -.
PeptideAtlas; Q80X90; -.
PRIDE; Q80X90; -.
Ensembl; ENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
GeneID; 286940; -.
KEGG; mmu:286940; -.
UCSC; uc007sek.1; mouse.
CTD; 2317; -.
MGI; MGI:2446089; Flnb.
eggNOG; KOG0518; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00900000140842; -.
HOGENOM; HOG000044235; -.
HOVERGEN; HBG004163; -.
InParanoid; Q80X90; -.
KO; K04437; -.
OMA; GTYDIFY; -.
OrthoDB; EOG091G00U5; -.
TreeFam; TF313685; -.
PRO; PR:Q80X90; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000025278; -.
CleanEx; MM_FLNB; -.
Genevisible; Q80X90; MM.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005925; C:focal adhesion; IDA:MGI.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001725; C:stress fiber; IDA:MGI.
GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
GO; GO:0003334; P:keratinocyte development; IMP:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 2.60.40.10; -; 24.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR001298; Filamin/ABP280_rpt.
InterPro; IPR029874; FLNB.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
PANTHER; PTHR43998:SF3; PTHR43998:SF3; 1.
Pfam; PF00307; CH; 2.
Pfam; PF00630; Filamin; 23.
SMART; SM00033; CH; 2.
SMART; SM00557; IG_FLMN; 24.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF81296; SSF81296; 24.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50194; FILAMIN_REPEAT; 24.
1: Evidence at protein level;
Acetylation; Actin-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Isopeptide bond; Phosphoprotein; Reference proteome;
Repeat; Ubl conjugation.
CHAIN 1 2602 Filamin-B.
/FTId=PRO_0000087299.
DOMAIN 16 122 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 139 242 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
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 1 239 Actin-binding.
REGION 1705 1728 Hinge 1. {ECO:0000250}.
REGION 2472 2602 Self-association site, tail.
{ECO:0000250}.
REGION 2472 2506 Hinge 2. {ECO:0000250}.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 519 519 Phosphothreonine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 681 681 N6-acetyllysine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 983 983 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1307 1307 Phosphothreonine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1316 1316 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1433 1433 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1505 1505 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1602 1602 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1780 1780 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2083 2083 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2113 2113 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2369 2369 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2465 2465 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2478 2478 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2481 2481 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2492 2492 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2518 2518 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2524 2524 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2576 2576 N6-acetyllysine.
{ECO:0000250|UniProtKB:O75369}.
CROSSLNK 2468 2468 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000250}.
SEQUENCE 2602 AA; 277825 MW; 41BA737EC52A89DB CRC64;
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK
RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP
GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK
GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP
VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK
AAGSGELGVT VKGPKGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC
TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG
IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK
DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY
DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG
PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ
VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV
AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD
GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE
GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT
GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN
GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL
GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK
NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV
IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP
DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN
HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD
YVLAVKWGEE HIPGSPFHVT VP


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