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O75369 (FLNB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Filamin-B
Short name=FLN-B
Alternative name(s):
ABP-278
ABP-280 homolog
Actin-binding-like protein
Beta-filamin
Filamin homolog 1
Short name=Fh1
Filamin-3
Thyroid autoantigen
Truncated actin-binding protein
Short name=Truncated ABP
Gene names
Name:FLNB
Synonyms:FLN1L, FLN3, TABP, TAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length2602 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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.

Subunit structure

Homodimer. Isoform 1 interacts with FBLP1, FLNA, FLNC, GP1BA, INPPL1, ITGB1A, PSEN1 and PSEN2. Isoform 3 interacts with ITGB1A, ITGB1D, ITGB3 and ITGB6. Interacts with MYOT and MYOZ1. Interacts with HBV capsid protein. Ref.1 Ref.2 Ref.3 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Isoform 1: Cytoplasm › cell cortex. Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › Z line. Note: In differentiating myotubes, isoform 1, isoform 2 and isoform 3 are localized diffusely throughout the cytoplasm with regions of enrichment at the longitudinal actin stress fiber. In differentiated tubes, isoform 1 is also detected within the Z-lines. Ref.1 Ref.3

Isoform 2: Cytoplasm › cytoskeleton. Note: Predominantly localized at actin stress fibers. Ref.1 Ref.3

Isoform 3: Cytoplasm › cytoskeleton. Note: Predominantly localized at actin stress fibers. Ref.1 Ref.3

Isoform 6: Cytoplasm › cytoskeleton. Note: Polarized at the periphery of myotubes. Ref.1 Ref.3

Tissue specificity

Ubiquitous. Isoform 1 and isoform 2 are expressed in placenta, bone marrow, brain, umbilical vein endothelial cells (HUVEC), retina and skeletal muscle. Isoform 1 is predominantly expressed in prostate, uterus, liver, thyroid, stomach, lymph node, small intestine, spleen, skeletal muscle, kidney, placenta, pancreas, heart, lung, platelets, endothelial cells, megakaryocytic and erythroleukemic cell lines. Isoform 2 is predominantly expressed in spinal cord, platelet and Daudi cells. Also expressed in thyroid adenoma, neurofibrillary tangles (NFT), senile plaques in the hippocampus and cerebral cortex in Alzheimer disease (AD). Isoform 3 and isoform 6 are expressed predominantly in lung, heart, skeletal muscle, testis, spleen, thymus and leukocytes. Isoform 4 and isoform 5 are expressed in heart. Ref.1 Ref.2 Ref.3 Ref.13

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.

Post-translational modification

ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling. Ref.24

Involvement in disease

Interaction with FLNA may compensate for dysfunctional FLNA homodimer in the periventricular nodular heterotopia (PVNH) disorder.

Atelosteogenesis 1 (AO1) [MIM:108720]: A lethal chondrodysplasia characterized by distal hypoplasia of the humeri and femurs, hypoplasia of the mid-thoracic spine, occasionally complete lack of ossification of single hand bones, and the finding in cartilage of multiple degenerated chondrocytes which are encapsulated in fibrous tissue.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32

Atelosteogenesis 3 (AO3) [MIM:108721]: A short-limb lethal skeletal dysplasia with vertebral abnormalities, disharmonious skeletal maturation, poorly modeled long bones and joint dislocations. Recurrent respiratory insufficiency and/or infections usually result in early death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32

Boomerang dysplasia (BOOMD) [MIM:112310]: Perinatal lethal osteochondrodysplasia characterized by absence or underossification of the limb bones and vertebrae. Boomerang dysplasia is distinguished from atelosteogenesis on the basis of a more severe defect in mineralisation, with complete absence of ossification in some limb elements and vertebral segments.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34

Larsen syndrome (LRS) [MIM:150250]: An osteochondrodysplasia characterized by large-joint dislocations and characteristic craniofacial abnormalities. The cardinal features of the condition are dislocations of the hip, knee and elbow joints, with equinovarus or equinovalgus foot deformities. Spatula-shaped fingers, most marked in the thumb, are also present. Craniofacial anomalies include hypertelorism, prominence of the forehead, a depressed nasal bridge, and a flattened midface. Cleft palate and short stature are often associated features. Spinal anomalies include scoliosis and cervical kyphosis. Hearing loss is a well-recognized complication.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32 Ref.36

Spondylocarpotarsal synostosis syndrome (SCT) [MIM:272460]: Disorder characterized by short stature and vertebral, carpal and tarsal fusions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32

Sequence similarities

Belongs to the filamin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 24 filamin repeats.

Sequence caution

The sequence AAA35505.1 differs from that shown. Reason: Frameshift at positions 2432 and 2589.

Ontologies

Keywords
   Biological processDifferentiation
Myogenesis
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   DomainRepeat
   LigandActin-binding
   Molecular functionDevelopmental protein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement Ref.13. Source: ProtInc

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

cytoskeletal anchoring at plasma membrane

Traceable author statement Ref.2. Source: ProtInc

skeletal muscle tissue development

Inferred from electronic annotation. Source: Compara

   Cellular_componentZ disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

actin cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: Compara

integral to membrane

Non-traceable author statement Ref.13. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

stress fiber

Inferred from electronic annotation. Source: Compara

   Molecular_functionactin binding

Non-traceable author statement Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75369-1)

Also known as: ABP-278;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75369-2)

Also known as: ABP-276;

The sequence of this isoform differs from the canonical sequence as follows:
     1704-1727: Missing.
Note: May be due to exon skipping.
Isoform 3 (identifier: O75369-3)

Also known as: Var-1;

The sequence of this isoform differs from the canonical sequence as follows:
     2081-2121: Missing.
Note: May be due to exon skipping.
Isoform 7 (identifier: O75369-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     170-181: ALGALVDSCAPG → MQEHSTRRRSLS
     1717-1727: Missing.
Isoform 4 (identifier: O75369-4)

Also known as: Var-3;

The sequence of this isoform differs from the canonical sequence as follows:
     2123-2150: EINSSDMSAHVTSPSGRVTEAEIVPMGK → GVRVMNCSAQILWGWRVQFHTGSRNQQQ
     2151-2602: Missing.
Isoform 5 (identifier: O75369-5)

Also known as: Var-2;

The sequence of this isoform differs from the canonical sequence as follows:
     2123-2146: EINSSDMSAHVTSPSGRVTEAEIV → GVRVMNCSAQILWGWRVQFHTGSR
     2147-2602: Missing.
Note: May be due to competing donor splice sites.
Isoform 6 (identifier: O75369-6)

Also known as: Var-1-DeltaH1;

The sequence of this isoform differs from the canonical sequence as follows:
     1704-1727: Missing.
     2081-2121: Missing.
Note: May be due to exon skipping.
Isoform 8 (identifier: O75369-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1463: R → RADDTDSQSWRSPLKALSEFFKGDPKGDFNKT
Isoform 9 (identifier: O75369-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1717-1727: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26022602Filamin-B
PRO_0000087298

Regions

Domain1 – 239239Actin-binding
Domain16 – 122107CH 1
Domain139 – 239101CH 2
Repeat249 – 34799Filamin 1
Repeat349 – 44698Filamin 2
Repeat447 – 54397Filamin 3
Repeat544 – 63693Filamin 4
Repeat640 – 73697Filamin 5
Repeat737 – 839103Filamin 6
Repeat840 – 93899Filamin 7
Repeat939 – 103496Filamin 8
Repeat1035 – 112793Filamin 9
Repeat1128 – 122295Filamin 10
Repeat1223 – 1322100Filamin 11
Repeat1323 – 141593Filamin 12
Repeat1416 – 151196Filamin 13
Repeat1512 – 160897Filamin 14
Repeat1609 – 170496Filamin 15
Repeat1729 – 181385Filamin 16
Repeat1816 – 190893Filamin 17
Repeat1919 – 199476Filamin 18
Repeat1997 – 208993Filamin 19
Repeat2091 – 218595Filamin 20
Repeat2188 – 228093Filamin 21
Repeat2282 – 237594Filamin 22
Repeat2379 – 247193Filamin 23
Repeat2507 – 260195Filamin 24
Region1128 – 1511384Interaction with FBLP1
Region1705 – 172824Hinge 1 By similarity
Region1862 – 2148287Interaction with the cytoplasmic tail of GP1BA
Region2060 – 2225166Interaction with FLNA 1
Region2130 – 2602473Interaction with INPPL1
Region2472 – 2602131Self-association site, tail By similarity
Region2472 – 250635Hinge 2 By similarity
Region2507 – 260296Interaction with FLNA 2

Amino acid modifications

Modified residue5191Phosphothreonine Ref.23 Ref.27
Modified residue6811N6-acetyllysine Ref.26
Modified residue7301Phosphoserine Ref.27
Modified residue8861Phosphoserine Ref.27
Modified residue9321Phosphoserine Ref.27
Modified residue9831Phosphoserine Ref.21 Ref.23 Ref.25 Ref.27
Modified residue10281Phosphoserine Ref.23
Modified residue13161Phosphoserine Ref.23 Ref.27
Modified residue14331Phosphoserine Ref.27
Modified residue15051Phosphoserine Ref.23
Modified residue15571Phosphothreonine By similarity
Modified residue16021Phosphoserine Ref.23
Modified residue20831Phosphoserine Ref.23
Modified residue21071Phosphoserine Ref.23
Modified residue23691Phosphoserine Ref.27
Modified residue24651Phosphoserine Ref.27
Modified residue24781Phosphoserine Ref.23 Ref.25 Ref.27
Modified residue24811Phosphoserine Ref.23
Modified residue25761N6-acetyllysine Ref.26
Cross-link2468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.24

Natural variations

Alternative sequence1 – 169169Missing in isoform 7.
VSP_024113
Alternative sequence170 – 18112ALGAL…SCAPG → MQEHSTRRRSLS in isoform 7.
VSP_024114
Alternative sequence14631R → RADDTDSQSWRSPLKALSEF FKGDPKGDFNKT in isoform 8.
VSP_043446
Alternative sequence1704 – 172724Missing in isoform 2 and isoform 6.
VSP_008773
Alternative sequence1717 – 172711Missing in isoform 7 and isoform 9.
VSP_024115
Alternative sequence2081 – 212141Missing in isoform 3 and isoform 6.
VSP_008774
Alternative sequence2123 – 215028EINSS…VPMGK → GVRVMNCSAQILWGWRVQFH TGSRNQQQ in isoform 4.
VSP_008775
Alternative sequence2123 – 214624EINSS…EAEIV → GVRVMNCSAQILWGWRVQFH TGSR in isoform 5.
VSP_008777
Alternative sequence2147 – 2602456Missing in isoform 5.
VSP_008778
Alternative sequence2151 – 2602452Missing in isoform 4.
VSP_008776
Natural variant1611F → C in LRS. Ref.32 Ref.36
VAR_033069
Natural variant1681G → S in LRS. Ref.36
VAR_033070
Natural variant1711L → R in BOOMD. Ref.34
VAR_033071
Natural variant1731A → V in AO1. Ref.32
Corresponds to variant rs28937586 [ dbSNP | Ensembl ].
VAR_033072
Natural variant1881S → P in AO1. Ref.32
VAR_033073
Natural variant2021M → V in AO1 and AO3. Ref.32
Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
VAR_033074
Natural variant2271E → K in LRS. Ref.32 Ref.36
VAR_033075
Natural variant2341L → V in LRS. Ref.36
VAR_033076
Natural variant2351S → P in BOOMD. Ref.34
VAR_033077
Natural variant3611G → S in LRS. Ref.36
VAR_033078
Natural variant3631G → E in LRS. Ref.36
VAR_033079
Natural variant5661R → Q in a breast cancer sample; somatic mutation. Ref.35
VAR_035917
Natural variant6631N → K in a breast cancer sample; somatic mutation. Ref.35
VAR_035918
Natural variant7031T → K in a breast cancer sample; somatic mutation. Ref.35
VAR_035919
Natural variant7511G → R in AO3. Ref.32
Corresponds to variant rs28937587 [ dbSNP | Ensembl ].
VAR_033080
Natural variant10181V → M.
Corresponds to variant rs2276742 [ dbSNP | Ensembl ].
VAR_017182
Natural variant11571D → N. Ref.1 Ref.4 Ref.5
Corresponds to variant rs1131356 [ dbSNP | Ensembl ].
VAR_017183
Natural variant11791E → K.
Corresponds to variant rs17058845 [ dbSNP | Ensembl ].
VAR_031392
Natural variant14311L → R in LRS. Ref.36
VAR_033081
Natural variant14711V → M. Ref.1 Ref.4 Ref.5
Corresponds to variant rs12632456 [ dbSNP | Ensembl ].
VAR_031393
Natural variant15341A → G in a breast cancer sample; somatic mutation. Ref.35
VAR_035920
Natural variant15711Missing in LRS. Ref.32 Ref.36
VAR_033082
Natural variant15861G → R in LRS. Ref.32 Ref.36
Corresponds to variant rs28939706 [ dbSNP | Ensembl ].
VAR_033083
Natural variant15921V → D in LRS. Ref.36
VAR_033084
Natural variant16031P → L in LRS. Ref.36
VAR_033085
Natural variant16911G → S in LRS. Ref.32 Ref.36
VAR_033086
Natural variant18341G → R in LRS. Ref.36
VAR_033087

Experimental info

Mutagenesis24681K → R: Cytoplasmic localization. Ref.24
Sequence conflict8161A → T in CAE46040. Ref.7
Sequence conflict9241Y → H in CAE46040. Ref.7
Sequence conflict14111F → L in CAE46040. Ref.7
Sequence conflict15601E → G in CAE46040. Ref.7
Sequence conflict19531L → F in AAF97046. Ref.4
Sequence conflict20061K → R in AAC33845. Ref.2
Sequence conflict20991I → S in CAE46040. Ref.7
Sequence conflict21701K → N in AAF97046. Ref.4
Sequence conflict22931M → V in AAF97046. Ref.4
Sequence conflict22931M → V in CAE46040. Ref.7
Sequence conflict23541V → A in CAB70818. Ref.11
Sequence conflict24871S → C in AAA35505. Ref.13
Sequence conflict25711V → A in CAB70818. Ref.11

Secondary structure

1 ............................................................................................................................................................................................................................................................................................................................................... 2602
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ABP-278) [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 1BF5C64C86360C6A

FASTA2,602278,164
        10         20         30         40         50         60 
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK 

        70         80         90        100        110        120 
RMYRKYHQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH 

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

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

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

       310        320        330        340        350        360 
EEAQVTPDSD KNKTYSVEYL PKVTGLHKVT VLFAGQHISK SPFEVSVDKA QGDASKVTAK 

       370        380        390        400        410        420 
GPGLEAVGNI ANKPTYFDIY TAGAGVGDIG VEVEDPQGKN TVELLVEDKG NQVYRCVYKP 

       430        440        450        460        470        480 
MQPGPHVVKI FFAGDTIPKS PFVVQVGEAC NPNACRASGR GLQPKGVRIR ETTDFKVDTK 

       490        500        510        520        530        540 
AAGSGELGVT MKGPKGLEEL VKQKDFLDGV YAFEYYPSTP GRYSIAITWG GHHIPKSPFE 

       550        560        570        580        590        600 
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG SLGFAIEGPS QAKIEYNDQN 

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

       670        680        690        700        710        720 
IVNNLAEFTV DPKDAGKAPL KIFAQDGEGQ RIDIQMKNRM DGTYACSYTP VKAIKHTIAV 

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

       790        800        810        820        830        840 
IKCDARVLSE DEEDVDFDII HNANDTFTVK YVPPAAGRYT IKVLFASQEI PASPFRVKVD 

       850        860        870        880        890        900 
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV YTKGAGKAPL NVQFNSPLPG DAVKDLDIID 

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

       970        980        990       1000       1010       1020 
DQEFTVDTRG AGGQGKLDVT ILSPSRKVVP CLVTPVTGRE NSTAKFIPRE EGLYAVDVTY 

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

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

      1150       1160       1170       1180       1190       1200 
PGLEHGKVGE AGLLSVDCSE AGPGALGLEA VSDSGTKAEV SIQNNKDGTY AVTYVPLTAG 

      1210       1220       1230       1240       1250       1260 
MYTLTMKYGG ELVPHFPARV KVEPAVDTSR IKVFGPGIEG KDVFREATTD FTVDSRPLTQ 

      1270       1280       1290       1300       1310       1320 
VGGDHIKAHI ANPSGASTEC FVTDNADGTY QVEYTPFEKG LHVVEVTYDD VPIPNSPFKV 

      1330       1340       1350       1360       1370       1380 
AVTEGCQPSR VQAQGPGLKE AFTNKPNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD 

      1390       1400       1410       1420       1430       1440 
GSCSAEYIPF APGDYDVNIT YGGAHIPGSP FRVPVKDVVD PSKVKIAGPG LGSGVRARVL 

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

      1510       1520       1530       1540       1550       1560 
EIPRSPFKVK VLPTYDASKV TASGPGLSSY GVPASLPVDF AIDARDAGEG LLAVQITDQE 

      1570       1580       1590       1600       1610       1620 
GKPKRAIVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDDIP LSPYRIRATQ TGDASKCLAT 

      1630       1640       1650       1660       1670       1680 
GPGIASTVKT GEEVGFVVDA KTAGKGKVTC TVLTPDGTEA EADVIENEDG TYDIFYTAAK 

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

      1750       1760       1770       1780       1790       1800 
GLGFKPFDLV IPFAVRKGEI TGEVHMPSGK TATPEIVDNK DGTVTVRYAP TEVGLHEMHI 

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

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

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

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

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

      2110       2120       2130       2140       2150       2160 
RTSRAPSVAT VGSICDLNLK IPEINSSDMS AHVTSPSGRV TEAEIVPMGK NSHCVRFVPQ 

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

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

      2290       2300       2310       2320       2330       2340 
IAPSDDARRL TVMSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP 

      2350       2360       2370       2380       2390       2400 
DKYAVRFIPH ENGVHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GTGLEGGTTG 

      2410       2420       2430       2440       2450       2460 
IQSEFFINTT RAGPGTLSVT IEGPSKVKMD CQETPEGYKV MYTPMAPGNY LISVKYGGPN 

      2470       2480       2490       2500       2510       2520 
HIVGSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKASS DASKVTSKGA 

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

      2590       2600 
YVLAVKWGEE HIPGSPFHVT VP

« Hide

Isoform 2 (ABP-276) [UniParc].

Checksum: 4E51115028A676F8
Show »

FASTA2,578275,668
Isoform 3 (Var-1) [UniParc].

Checksum: A367021E1BCF1EF1
Show »

FASTA2,561273,909
Isoform 7 [UniParc].

Checksum: 8BB43D0D58E153B1
Show »

FASTA2,422257,551
Isoform 4 (Var-3) [UniParc].

Checksum: B1FDAE6F0E99947C
Show »

FASTA2,150230,788
Isoform 5 (Var-2) [UniParc].

Checksum: 0E99947C9734D59E
Show »

FASTA2,146230,289
Isoform 6 (Var-1-DeltaH1) [UniParc].

Checksum: DABD7554C44F38DA
Show »

FASTA2,537271,413
Isoform 8 [UniParc].

Checksum: 8D8F7817049EECA1
Show »

FASTA2,633281,635
Isoform 9 [UniParc].

Checksum: 2D9AF6AF4D1469EF
Show »

FASTA2,591276,939

References

« Hide 'large scale' references
[1]"Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha."
Takafuta T., Wu G., Murphy G.F., Shapiro S.S.
J. Biol. Chem. 273:17531-17538(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH GP1BA, VARIANTS ASN-1157 AND MET-1471.
Tissue: Endothelial cell and Placenta.
[2]"A novel human actin-binding protein homologue that binds to platelet glycoprotein Ibalpha."
Xu W.-F., Xie Z.-W., Chung D.W., Davie E.W.
Blood 92:1268-1276(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH GP1BA.
Tissue: Placenta.
[3]"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 [GENOMIC DNA] (ISOFORMS 1; 3; 4 AND 5), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ISOFORMS OF ITGB1.
Tissue: Keratinocyte and Skeletal muscle.
[4]"Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family."
Chakarova C., Wehnert M.S., Uhl K., Sakthivel S., Vosberg H.-P., van der Ven P.F.M., Fuerst D.O.
Hum. Genet. 107:597-611(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GENE ORGANIZATION, SIMILARITY TO OTHER MEMBERS OF THE FAMILY, VARIANTS ASN-1157 AND MET-1471.
[5]"Fine expression profiling of full-length transcripts using a size-unbiased cDNA library prepared with the vector-capping method."
Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.
DNA Res. 15:123-136(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 8 AND 9), VARIANTS ASN-1157 AND MET-1471.
[6]"Vector-capping: a simple method for preparing a high-quality full-length cDNA library."
Kato S., Ohtoko K., Ohtake H., Kimura T.
DNA Res. 12:53-62(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 8 AND 9).
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Endometrial tumor and Fetal brain.
[8]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 990-2602.
Tissue: Aortic endothelium.
[10]"The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin."
Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C., Coghill I.D., Nandurkar H.H., Ooms L.M., Mitchell C.A.
J. Cell Biol. 155:1065-1079(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2130-2602, INTERACTION WITH INPPL1.
Tissue: Skeletal muscle.
[11]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1874-2602.
Tissue: Fetal brain.
[12]"Interaction of presenilins with the filamin family of actin-binding proteins."
Zhang W., Han S.W., McKeel D.W., Goate A., Wu J.Y.
J. Neurosci. 18:914-922(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2311-2602, INTERACTION WITH PSEN1 AND PSEN2.
Tissue: Fetal brain.
[13]"Cloning from the thyroid of a protein related to actin binding protein that is recognized by Graves disease immunoglobulins."
Leedman P.J., Faulkner-Jones B., Cram D.C., Harrison P.J., West J., O'Brien E.J., Simpson R., Coppel R.L., Harrison L.C.
Proc. Natl. Acad. Sci. U.S.A. 90:5994-5998(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2404-2602, TISSUE SPECIFICITY.
Tissue: Thyroid.
[14]"Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein."
Huang C.J., Chen Y.H., Ting L.P.
J. Biomed. Sci. 7:160-168(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HBV CAPSID PROTEIN.
[15]"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: INTERACTION WITH FLNA.
[16]"A new member of the LIM protein family binds to filamin B and localizes at stress fibers."
Takafuta T., Saeki M., Fujimoto T.-T., Fujimura K., Shapiro S.S.
J. Biol. Chem. 278:12175-12181(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLP1.
Tissue: Placenta.
[17]"The limits of promiscuity: isoform-specific dimerization of filamins."
Himmel M., van der Ven P.F.M., Stoecklein W., Fuerst D.O.
Biochemistry 42:430-439(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DIMERIZATION, INTERACTION WITH FLNC.
[18]"The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins."
Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L.
J. Cell Sci. 118:3739-3749(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1; MYOT AND MYOZ1.
[19]"Structural and functional aspects of filamins."
van der Flier A., Sonnenberg A.
Biochim. Biophys. Acta 1538:99-117(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[20]"Filamins as integrators of cell mechanics and signalling."
Stossel T.P., Condeelis J., Cooley L., Hartwig J.H., Noegel A., Schleicher M., Shapiro S.S.
Nat. Rev. Mol. Cell Biol. 2:138-145(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[21]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[22]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-983; SER-1028; SER-1316; SER-1505; SER-1602; SER-2083; SER-2107; SER-2478 AND SER-2481, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"ISG15 modification of filamin B negatively regulates the type I interferon-induced JNK signalling pathway."
Jeon Y.J., Choi J.S., Lee J.Y., Yu K.R., Kim S.M., Ka S.H., Oh K.H., Kim K.I., Zhang D.E., Bang O.S., Chung C.H.
EMBO Rep. 10:374-380(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION AT LYS-2468, MUTAGENESIS OF LYS-2468.
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2478, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[26]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681 AND LYS-2576, MASS SPECTROMETRY.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-730; SER-886; SER-932; SER-983; SER-1316; SER-1433; SER-2369; SER-2465 AND SER-2478, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Disease-associated substitutions in the filamin B actin binding domain confer enhanced actin binding affinity in the absence of major structural disturbance: Insights from the crystal structures of filamin B actin binding domains."
Sawyer G.M., Clark A.R., Robertson S.P., Sutherland-Smith A.J.
J. Mol. Biol. 390:1030-1047(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-242.
[31]"Solution structure of the 9th through 24th filamin domains from human filamin-B."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1017-1721; 1736-2488 AND 2509-2602.
[32]"Mutations in the gene encoding filamin B disrupt vertebral segmentation, joint formation and skeletogenesis."
Krakow D., Robertson S.P., King L.M., Morgan T., Sebald E.T., Bertolotto C., Wachsmann-Hogiu S., Acuna D., Shapiro S.S., Takafuta T., Aftimos S., Kim C.A., Firth H., Steiner C.E., Cormier-Daire V., Superti-Furga A., Bonafe L., Graham J.M. Jr. expand/collapse author list , Grix A., Bacino C.A., Allanson J., Bialer M.G., Lachman R.S., Rimoin D.L., Cohn D.H.
Nat. Genet. 36:405-410(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCT, VARIANTS LRS CYS-161; LYS-227; ASN-1571 DEL; ARG-1586 AND SER-1691, VARIANTS AO1 VAL-173 AND PRO-188, VARIANT AO3 ARG-751, VARIANT AO1/AO3 VAL-202.
[33]"Solution structure of filamin domains from human filamin-B."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1017-2602.
[34]"Mutations in FLNB cause boomerang dysplasia."
Bicknell L.S., Morgan T., Bonafe L., Wessels M.W., Bialer M.G., Willems P.J., Cohn D.H., Krakow D., Robertson S.P.
J. Med. Genet. 42:E43-E43(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BOOMD ARG-171 AND PRO-235.
[35]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-566; LYS-663; LYS-703 AND GLY-1534.
[36]"A molecular and clinical study of Larsen syndrome caused by mutations in FLNB."
Bicknell L.S., Farrington-Rock C., Shafeghati Y., Rump P., Alanay Y., Alembik Y., Al-Madani N., Firth H., Karimi-Nejad M.H., Kim C.A., Leask K., Maisenbacher M., Moran E., Pappas J.G., Prontera P., de Ravel T., Fryns J.-P., Sweeney E. expand/collapse author list , Fryer A., Unger S., Wilson L.C., Lachman R.S., Rimoin D.L., Cohn D.H., Krakow D., Robertson S.P.
J. Med. Genet. 44:89-98(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LRS CYS-161; SER-168; LYS-227; VAL-234; SER-361; GLU-363; ARG-1431; ASN-1571 DEL; ARG-1586; ASP-1592; LEU-1603; SER-1691 AND ARG-1834.
+Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF042166 mRNA. Translation: AAC39842.1.
AF043045 mRNA. Translation: AAC33845.1.
AF353667 Genomic DNA. Translation: AAL68440.1.
AF353667 Genomic DNA. Translation: AAL68441.1.
AF353667 Genomic DNA. Translation: AAL68442.1.
AF353667 Genomic DNA. Translation: AAL68443.1.
AF191633 expand/collapse EMBL AC list , AF191594, AF191595, AF191596, AF191597, AF191598, AF191599, AF191600, AF191601, AF191602, AF191603, AF191604, AF191605, AF191606, AF191607, AF191608, AF191609, AF191611, AF191610, AF191613, AF191612, AF191614, AF191615, AF191617, AF191616, AF191618, AF191619, AF191620, AF191621, AF191622, AF191623, AF191624, AF191625, AF191627, AF191626, AF191628, AF191629, AF191630, AF191631, AF191632 Genomic DNA. Translation: AAF72339.1.
AF238609 mRNA. Translation: AAF97046.1.
AB371580 mRNA. Translation: BAG48309.1.
AB371581 mRNA. Translation: BAG48310.1.
AB371582 mRNA. Translation: BAG48311.1.
AB191258 mRNA. Translation: BAD52434.1.
BX641085 mRNA. Translation: CAE46040.1.
AC114399 Genomic DNA. No translation available.
AC137936 Genomic DNA. No translation available.
AL137574 mRNA. Translation: CAB70818.1.
AB209889 mRNA. Translation: BAD93126.1.
M62994 mRNA. Translation: AAA35505.1. Frameshift.
IPIIPI00289334.
IPI00382697.
IPI00382698.
IPI00382699.
IPI00477536.
IPI00900293.
IPI00940093.
IPI00943563.
IPI00953109.
PIRT46270.
RefSeqNP_001157789.1. NM_001164317.1.
NP_001157790.1. NM_001164318.1.
NP_001157791.1. NM_001164319.1.
NP_001448.2. NM_001457.3.
UniGeneHs.476448.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DI8NMR-A1999-2096[»]
2DI9NMR-A1017-1134[»]
2DIANMR-A1130-1229[»]
2DIBNMR-A1215-1329[»]
2DICNMR-A1325-1422[»]
2DJ4NMR-A1418-1518[»]
2DLGNMR-A2104-2192[»]
2DMBNMR-A1611-1721[»]
2DMCNMR-A1899-2001[»]
2E9INMR-A2094-2192[»]
2E9JNMR-A1504-1615[»]
2EE6NMR-A2190-2287[»]
2EE9NMR-A1736-1823[»]
2EEANMR-A1808-1915[»]
2EEBNMR-A2284-2382[»]
2EECNMR-A2371-2488[»]
2EEDNMR-A2509-2602[»]
2WA5X-ray1.90A2-242[»]
2WA6X-ray1.95A2-242[»]
2WA7X-ray1.85A2-242[»]
3FERX-ray2.40A/B/C/D1-252[»]
4B7LX-ray2.05A/B1-347[»]
ProteinModelPortalO75369.
SMRO75369. Positions 13-634, 639-2602.
ModBaseSearch...

Protein-protein interaction databases

IntActO75369. 18 interactions.
MINTMINT-4998813.

PTM databases

PhosphoSiteO75369.

Proteomic databases

PaxDbO75369.
PRIDEO75369.

Protocols and materials databases

DNASU2317.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295956; ENSP00000295956; ENSG00000136068.
ENST00000348383; ENSP00000232447; ENSG00000136068.
ENST00000357272; ENSP00000349819; ENSG00000136068.
ENST00000358537; ENSP00000351339; ENSG00000136068.
ENST00000419752; ENSP00000414532; ENSG00000136068.
ENST00000429972; ENSP00000415599; ENSG00000136068.
ENST00000490882; ENSP00000420213; ENSG00000136068.
GeneID2317.
KEGGhsa:2317.
UCSCuc003djj.2. human.
uc003djl.2. human.
uc010hnf.2. human.

Organism-specific databases

CTD2317.
GeneCardsGC03P057969.
H-InvDBHIX0003397.
HGNCHGNC:3755. FLNB.
HPACAB019322.
HPA004747.
HPA004886.
MIM108720. phenotype.
108721. phenotype.
112310. phenotype.
150250. phenotype.
272460. phenotype.
603381. gene.
neXtProtNX_O75369.
Orphanet1190. Atelosteogenesis I.
56305. Atelosteogenesis type III.
503. Autosomal dominant Larsen syndrome.
1263. Boomerang dysplasia.
3275. Synspondylism.
PharmGKBPA28173.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000044235.
HOVERGENHBG004163.
InParanoidO75369.
KOK04437.
OMAHIMCDDE.
OrthoDBEOG4V436R.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO75369.
BgeeO75369.
GenevestigatorO75369.
GermOnlineENSG00000136068. Homo sapiens.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001298. Filamin.
IPR017868. Filamin/ABP280_repeat-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMSSF47576. Calponin-homology. 1 hit.
SSF81296. Ig_E-set. 24 hits.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFLNB. human.
EvolutionaryTraceO75369.
GenomeRNAi2317.
NextBio9409.
SOURCESearch...

Entry information

Entry nameFLNB_HUMAN
AccessionPrimary (citable) accession number: O75369
Secondary accession number(s): B2ZZ83 expand/collapse secondary AC list , B2ZZ84, B2ZZ85, C9JKE6, C9JMC4, Q13706, Q59EC2, Q60FE7, Q6MZJ1, Q8WXS9, Q8WXT0, Q8WXT1, Q8WXT2, Q9NRB5, Q9NT26, Q9UEV9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 18, 2010
Last modified: May 1, 2013
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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