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Protein

Filamin-B

Gene

Flnb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • epithelial cell morphogenesis Source: MGI
  • keratinocyte development Source: MGI
  • skeletal muscle tissue development Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-1169408. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Filamin-B
Short name:
FLN-B
Alternative name(s):
ABP-280-like protein
Actin-binding-like protein
Beta-filamin
Gene namesi
Name:Flnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:2446089. Flnb.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: UniProtKB
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • plasma membrane Source: MGI
  • stress fiber Source: MGI
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26022602Filamin-BPRO_0000087299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161PhosphothreonineBy similarity
Modified residuei519 – 5191PhosphothreonineBy similarity
Modified residuei681 – 6811N6-acetyllysineBy similarity
Modified residuei730 – 7301PhosphoserineBy similarity
Modified residuei886 – 8861PhosphoserineBy similarity
Modified residuei932 – 9321PhosphoserineBy similarity
Modified residuei983 – 9831PhosphoserineBy similarity
Modified residuei1028 – 10281PhosphoserineBy similarity
Modified residuei1307 – 13071PhosphothreonineBy similarity
Modified residuei1316 – 13161PhosphoserineBy similarity
Modified residuei1433 – 14331PhosphoserineBy similarity
Modified residuei1505 – 15051PhosphoserineBy similarity
Modified residuei1602 – 16021PhosphoserineBy similarity
Modified residuei1780 – 17801N6-acetyllysineCombined sources
Modified residuei2083 – 20831PhosphoserineBy similarity
Modified residuei2113 – 21131PhosphoserineBy similarity
Modified residuei2369 – 23691PhosphoserineBy similarity
Modified residuei2465 – 24651PhosphoserineBy similarity
Cross-linki2468 – 2468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)By similarity
Modified residuei2478 – 24781PhosphoserineBy similarity
Modified residuei2481 – 24811PhosphoserineBy similarity
Modified residuei2492 – 24921PhosphoserineBy similarity
Modified residuei2518 – 25181N6-succinyllysineCombined sources
Modified residuei2524 – 25241N6-succinyllysineCombined sources
Modified residuei2576 – 25761N6-acetyllysineBy similarity

Post-translational modificationi

ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling.By similarity
Ubiquitination by a SCF-like complex containing ASB2 isoform 2 leads to proteasomal degradation which promotes muscle differentiation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ80X90.
MaxQBiQ80X90.
PaxDbiQ80X90.
PRIDEiQ80X90.

PTM databases

iPTMnetiQ80X90.
PhosphoSiteiQ80X90.

Expressioni

Tissue specificityi

Expressed in hippocampus, cortex, cerebellar Purkinje cells and granule cell layers.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ80X90.
CleanExiMM_FLNB.
GenevisibleiQ80X90. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A, ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By similarity). Interacts with MICALL2. Interacts with FAM101A and FAM101B (PubMed:21709252,PubMed:24436304).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi235046. 104 interactions.
IntActiQ80X90. 106 interactions.
MINTiMINT-1866796.
STRINGi10090.ENSMUSP00000052020.

Structurei

3D structure databases

ProteinModelPortaliQ80X90.
SMRiQ80X90. Positions 13-347, 450-739, 1017-1723, 1735-2488, 2511-2602.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 239239Actin-bindingAdd
BLAST
Domaini16 – 122107CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 239101CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati249 – 34799Filamin 1Add
BLAST
Repeati349 – 44698Filamin 2Add
BLAST
Repeati447 – 54397Filamin 3Add
BLAST
Repeati544 – 63693Filamin 4Add
BLAST
Repeati640 – 73697Filamin 5Add
BLAST
Repeati737 – 839103Filamin 6Add
BLAST
Repeati840 – 93899Filamin 7Add
BLAST
Repeati939 – 103496Filamin 8Add
BLAST
Repeati1035 – 112793Filamin 9Add
BLAST
Repeati1128 – 122295Filamin 10Add
BLAST
Repeati1223 – 1322100Filamin 11Add
BLAST
Repeati1323 – 141593Filamin 12Add
BLAST
Repeati1416 – 151196Filamin 13Add
BLAST
Repeati1512 – 160897Filamin 14Add
BLAST
Repeati1609 – 170496Filamin 15Add
BLAST
Repeati1729 – 181385Filamin 16Add
BLAST
Repeati1816 – 190893Filamin 17Add
BLAST
Repeati1919 – 199476Filamin 18Add
BLAST
Repeati1997 – 208993Filamin 19Add
BLAST
Repeati2091 – 218595Filamin 20Add
BLAST
Repeati2188 – 228093Filamin 21Add
BLAST
Repeati2282 – 237594Filamin 22Add
BLAST
Repeati2379 – 247193Filamin 23Add
BLAST
Repeati2507 – 260195Filamin 24Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1705 – 172824Hinge 1By similarityAdd
BLAST
Regioni2472 – 2602131Self-association site, tailBy similarityAdd
BLAST
Regioni2472 – 250635Hinge 2By similarityAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the filamin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 24 filamin repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOGENOMiHOG000044235.
HOVERGENiHBG004163.
InParanoidiQ80X90.
KOiK04437.
OMAiDFKVDTK.
OrthoDBiEOG76T9QC.
TreeFamiTF313685.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR029874. FLNB.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF238. PTHR11915:SF238. 1 hit.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80X90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL
60 70 80 90 100
IALLEVLSQK RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK
110 120 130 140 150
AIVDGNLKLI LGLVWTLILH YSISMPVWED EGDDDAKKQT PKQRLLGWIQ
160 170 180 190 200
NKIPYLPITN FNQNWQDGKA LGALVDSCAP GLCPDWESWD PRKPVDNARE
210 220 230 240 250
AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA KLKPGAPLKP
260 270 280 290 300
KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
310 320 330 340 350
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA
360 370 380 390 400
QGDASKVTAK GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN
410 420 430 440 450
SVELLVEDRG NQVYRCVYKP VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC
460 470 480 490 500
NPNACRASGR GLQPKGVRIR ETADFKVDTK AAGSGELGVT VKGPKGLEEL
510 520 530 540 550
VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE VQVGPEAGMQ
560 570 580 590 600
KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN
610 620 630 640 650
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA
660 670 680 690 700
YGPGLEKSGC TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM
710 720 730 740 750
DGTYACSYTP LKAIKHTIAV VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP
760 770 780 790 800
GVERSGLKAN EPTHFTVDCT EAGEGDVSVG IKCDARVLSD DEEDVDFDII
810 820 830 840 850
HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD PSHDASKVKA
860 870 880 890 900
EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID
910 920 930 940 950
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN
960 970 980 990 1000
GLENRVEVGK DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE
1010 1020 1030 1040 1050
CSTAKFIPRE EGLFAVDVTY DGHPVPGSPY TVEASLPPDP TKVKAHGPGL
1060 1070 1080 1090 1100
EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP CEAKIECSDN GDGTCSVSYL
1110 1120 1130 1140 1150
PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG PGLEHGKVGE
1160 1170 1180 1190 1200
PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG
1210 1220 1230 1240 1250
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD
1260 1270 1280 1290 1300
FTVDSRPLTQ VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG
1310 1320 1330 1340 1350
FHVVEVTYDD VPIPNSPFKV AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT
1360 1370 1380 1390 1400
VVTRGAGIGG LGITVEGPSE SKINCRDNKD GSCSAEYIPF APGDYDVNIT
1410 1420 1430 1440 1450
YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP QSFTVDSSKA
1460 1470 1480 1490 1500
GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE
1510 1520 1530 1540 1550
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG
1560 1570 1580 1590 1600
LLAVQITDQE GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP
1610 1620 1630 1640 1650
LSPYRIRATQ TGDASKCLAT GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC
1660 1670 1680 1690 1700
VILTPDGTEA EADVIENEDG TYDIFYTAAK PGTYVIYVRF GGVDIPNSPF
1710 1720 1730 1740 1750
TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN GLGFKPFDLV
1760 1770 1780 1790 1800
IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI
1810 1820 1830 1840 1850
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG
1860 1870 1880 1890 1900
EGGLDLAIEG PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP
1910 1920 1930 1940 1950
GSPFTAKITD DNRRCSQVKL GSAADFLLDI SETDLSTLTA SIKAPSGRDE
1960 1970 1980 1990 2000
PCLLKRLPNN HIGISFIPRE VGEHLVSIKK NGNHVANSPV SIMVVQSEIG
2010 2020 2030 2040 2050
DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE GPSKVDIQTE
2060 2070 2080 2090 2100
DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT
2110 2120 2130 2140 2150
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK
2160 2170 2180 2190 2200
NSHCVRFVPQ EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG
2210 2220 2230 2240 2250
PGLERGEAGI PAEFSIWTRE AGAGGLSIAV EGPSKAEITF DDHKNGSCGV
2260 2270 2280 2290 2300
SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV IAPSDDARCL TVLSLQESGL
2310 2320 2330 2340 2350
KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP DKYAVRFIPH
2360 2370 2380 2390 2400
ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG
2410 2420 2430 2440 2450
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY
2460 2470 2480 2490 2500
LIGVKYGGPN HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET
2510 2520 2530 2540 2550
CYSAIPKSSS DASKVTSKGA GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH
2560 2570 2580 2590 2600
GPTTPCEEVS MKHVGKQQYN VTYVVKERGD YVLAVKWGEE HIPGSPFHVT

VP
Length:2,602
Mass (Da):277,825
Last modified:July 27, 2011 - v3
Checksum:i41BA737EC52A89DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC129222 Genomic DNA. No translation available.
AC140322 Genomic DNA. No translation available.
AF353669 mRNA. Translation: AAL68445.1.
AF353672 mRNA. Translation: AAL68448.1.
BC003959 mRNA. Translation: AAH03959.1.
BC048835 mRNA. Translation: AAH48835.1.
CCDSiCCDS70540.1.
RefSeqiNP_001074896.1. NM_001081427.1.
UniGeneiMm.489652.

Genome annotation databases

EnsembliENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
GeneIDi286940.
KEGGimmu:286940.
UCSCiuc007sek.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC129222 Genomic DNA. No translation available.
AC140322 Genomic DNA. No translation available.
AF353669 mRNA. Translation: AAL68445.1.
AF353672 mRNA. Translation: AAL68448.1.
BC003959 mRNA. Translation: AAH03959.1.
BC048835 mRNA. Translation: AAH48835.1.
CCDSiCCDS70540.1.
RefSeqiNP_001074896.1. NM_001081427.1.
UniGeneiMm.489652.

3D structure databases

ProteinModelPortaliQ80X90.
SMRiQ80X90. Positions 13-347, 450-739, 1017-1723, 1735-2488, 2511-2602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi235046. 104 interactions.
IntActiQ80X90. 106 interactions.
MINTiMINT-1866796.
STRINGi10090.ENSMUSP00000052020.

PTM databases

iPTMnetiQ80X90.
PhosphoSiteiQ80X90.

Proteomic databases

EPDiQ80X90.
MaxQBiQ80X90.
PaxDbiQ80X90.
PRIDEiQ80X90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
GeneIDi286940.
KEGGimmu:286940.
UCSCiuc007sek.1. mouse.

Organism-specific databases

CTDi2317.
MGIiMGI:2446089. Flnb.

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOGENOMiHOG000044235.
HOVERGENiHBG004163.
InParanoidiQ80X90.
KOiK04437.
OMAiDFKVDTK.
OrthoDBiEOG76T9QC.
TreeFamiTF313685.

Enzyme and pathway databases

ReactomeiR-MMU-1169408. ISG15 antiviral mechanism.

Miscellaneous databases

PROiQ80X90.
SOURCEiSearch...

Gene expression databases

BgeeiQ80X90.
CleanExiMM_FLNB.
GenevisibleiQ80X90. MM.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR029874. FLNB.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF238. PTHR11915:SF238. 1 hit.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
    van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
    J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1663-1752 AND 2031-2181.
    Strain: C3H/HeJ.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1884-2602.
    Strain: FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  4. "Filamin A and filamin B are co-expressed within neurons during periods of neuronal migration and can physically interact."
    Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.
    Hum. Mol. Genet. 11:2845-2854(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    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.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "RefilinB (FAM101B) targets filamin A to organize perinuclear actin networks and regulates nuclear shape."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 108:11464-11469(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM101A AND FAM101B.
  8. "Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins."
    Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., Imoto I., Matsushita N., Sasaki T.
    Genes Cells 18:810-822(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICALL2.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1780, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-2518 AND LYS-2524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the formation of cartilaginous skeletal elements."
    Mizuhashi K., Kanamoto T., Moriishi T., Muranishi Y., Miyazaki T., Terada K., Omori Y., Ito M., Komori T., Furukawa T.
    Hum. Mol. Genet. 23:2953-2967(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM101A AND FAM101B.

Entry informationi

Entry nameiFLNB_MOUSE
AccessioniPrimary (citable) accession number: Q80X90
Secondary accession number(s): E9QNV9
, Q8VHX4, Q8VHX7, Q99KY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: July 27, 2011
Last modified: April 13, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.