Filamin-B - Mus musculus (Mouse)

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Q80X90 (FLNB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Filamin-B
Short name=FLN-B

Alternative name(s):
ABP-280-like protein
Actin-binding-like protein
Beta-filamin

Gene names

Name:

Flnb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2602 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A, ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 By similarity.
Subcellular location	Cytoplasm › cell cortex. Cytoplasm › myofibril › sarcomere › Z line By similarity. Cytoplasm › cytoskeleton. Note: May localize also at actin stress fibers and within the Z-lines By similarity.
Tissue specificity	Expressed in hippocampus, cortex, cerebellar Purkinje cells and granule cell layers. Ref.4
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. Ref.4
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.
Post-translational modification	ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling By similarity.
Sequence similarities	Belongs to the filamin family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 24 filamin repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat
Ligand	Actin-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	skeletal muscle tissue development Inferred from direct assay Ref.2. Source: MGI
Cellular_component	Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from sequence alignment Ref.4. Source: MGI focal adhesion Inferred from direct assay Ref.2. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara stress fiber Inferred from direct assay Ref.2. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2602

2602

Filamin-B

PRO_0000087299

Regions

Domain

1 – 239

239

Actin-binding

Domain

16 – 122

107

CH 1

Domain

139 – 239

101

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

103

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

100

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

131

Self-association site, tail By similarity

Region

2472 – 2506

Hinge 2 By similarity

Amino acid modifications

Modified residue

519

Phosphothreonine By similarity

Modified residue

681

N6-acetyllysine By similarity

Modified residue

730

Phosphoserine By similarity

Modified residue

886

Phosphoserine By similarity

Modified residue

932

Phosphoserine By similarity

Modified residue

983

Phosphoserine By similarity

Modified residue

1028

Phosphoserine By similarity

Modified residue

1316

Phosphoserine By similarity

Modified residue

1433

Phosphoserine By similarity

Modified residue

1505

Phosphoserine By similarity

Modified residue

1557

Phosphothreonine Ref.5

Modified residue

1602

Phosphoserine By similarity

Modified residue

2083

Phosphoserine By similarity

Modified residue

2369

Phosphoserine By similarity

Modified residue

2465

Phosphoserine By similarity

Modified residue

2478

Phosphoserine By similarity

Modified residue

2481

Phosphoserine By similarity

Modified residue

2576

N6-acetyllysine By similarity

Cross-link

2468

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q80X90 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 41BA737EC52A89DB
Show »

FASTA

2,602

277,825

        10         20         30         40         50         60 
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK 

        70         80         90        100        110        120 
RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH 

       130        140        150        160        170        180 
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP 

       190        200        210        220        230        240 
GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA 

       250        260        270        280        290        300 
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK 

       310        320        330        340        350        360 
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK 

       370        380        390        400        410        420 
GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP 

       430        440        450        460        470        480 
VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK 

       490        500        510        520        530        540 
AAGSGELGVT VKGPKGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE 

       550        560        570        580        590        600 
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN 

       610        620        630        640        650        660 
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC 

       670        680        690        700        710        720 
TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV 

       730        740        750        760        770        780 
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG 

       790        800        810        820        830        840 
IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD 

       850        860        870        880        890        900 
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID 

       910        920        930        940        950        960 
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK 

       970        980        990       1000       1010       1020 
DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY 

      1030       1040       1050       1060       1070       1080 
DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP 

      1090       1100       1110       1120       1130       1140 
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG 

      1150       1160       1170       1180       1190       1200 
PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG 

      1210       1220       1230       1240       1250       1260 
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ 

      1270       1280       1290       1300       1310       1320 
VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV 

      1330       1340       1350       1360       1370       1380 
AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD 

      1390       1400       1410       1420       1430       1440 
GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP 

      1450       1460       1470       1480       1490       1500 
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE 

      1510       1520       1530       1540       1550       1560 
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE 

      1570       1580       1590       1600       1610       1620 
GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT 

      1630       1640       1650       1660       1670       1680 
GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK 

      1690       1700       1710       1720       1730       1740 
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN 

      1750       1760       1770       1780       1790       1800 
GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI 

      1810       1820       1830       1840       1850       1860 
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG 

      1870       1880       1890       1900       1910       1920 
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL 

      1930       1940       1950       1960       1970       1980 
GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK 

      1990       2000       2010       2020       2030       2040 
NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE 

      2050       2060       2070       2080       2090       2100 
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT 

      2110       2120       2130       2140       2150       2160 
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ 

      2170       2180       2190       2200       2210       2220 
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE 

      2230       2240       2250       2260       2270       2280 
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV 

      2290       2300       2310       2320       2330       2340 
IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP 

      2350       2360       2370       2380       2390       2400 
DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG 

      2410       2420       2430       2440       2450       2460 
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN 

      2470       2480       2490       2500       2510       2520 
HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA 

      2530       2540       2550       2560       2570       2580 
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD 

      2590       2600 
YVLAVKWGEE HIPGSPFHVT VP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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.
[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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1557, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00663627.
UniGene	Mm.489652.
3D structure databases
ProteinModelPortal	Q80X90.
SMR	Q80X90. Positions 13-347, 1017-1723, 1735-2488, 2511-2602.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q80X90. 6 interactions.
MINT	MINT-1866796.
PTM databases
PhosphoSite	Q80X90.
Proteomic databases
PaxDb	Q80X90.
PRIDE	Q80X90.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
UCSC	uc007sek.1. mouse.
Organism-specific databases
MGI	MGI:2446089. Flnb.
Phylogenomic databases
eggNOG	COG5069.
GeneTree	ENSGT00660000095431.
HOGENOM	HOG000044235.
HOVERGEN	HBG004163.
InParanoid	Q80X90.
OMA	HIMCDDE.
OrthoDB	EOG4V436R.
Gene expression databases
ArrayExpress	Q80X90.
Bgee	Q80X90.
CleanEx	MM_FLNB.
Genevestigator	Q80X90.
GermOnline	ENSMUSG00000025278. Mus musculus.
Family and domain databases
Gene3D	1.10.418.10. 2 hits. 2.60.40.10. 24 hits.
InterPro	IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR001298. Filamin. IPR017868. Filamin/ABP280_repeat-like. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. [Graphical view]
Pfam	PF00307. CH. 2 hits. PF00630. Filamin. 23 hits. [Graphical view]
SMART	SM00033. CH. 2 hits. SM00557. IG_FLMN. 24 hits. [Graphical view]
SUPFAM	SSF47576. Calponin-homology. 1 hit. SSF81296. Ig_E-set. 24 hits.
PROSITE	PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. PS50194. FILAMIN_REPEAT. 24 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

FLNB_MOUSE

Accession

Primary (citable) accession number: Q80X90
Secondary accession number(s): E9QNV9

Q99KY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents