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O75369

- FLNB_HUMAN

UniProt

O75369 - FLNB_HUMAN

Protein

Filamin-B

Gene

FLNB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    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. 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.

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. cell differentiation Source: UniProtKB-KW
    3. cytokine-mediated signaling pathway Source: Reactome
    4. cytoskeletal anchoring at plasma membrane Source: ProtInc
    5. signal transduction Source: ProtInc
    6. skeletal muscle tissue development Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Myogenesis

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    SignaLinkiO75369.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:FLNB
    Synonyms:FLN1L, FLN3, TABP, TAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3755. FLNB.

    Subcellular locationi

    Isoform 1 : Cytoplasmcell cortex. Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ 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.
    Isoform 2 : Cytoplasmcytoskeleton
    Note: Predominantly localized at actin stress fibers.
    Isoform 3 : Cytoplasmcytoskeleton
    Note: Predominantly localized at actin stress fibers.
    Isoform 6 : Cytoplasmcytoskeleton
    Note: Polarized at the periphery of myotubes.

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cell cortex Source: UniProtKB-SubCell
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. focal adhesion Source: Ensembl
    7. integral component of membrane Source: UniProtKB
    8. plasma membrane Source: HPA
    9. stress fiber Source: Ensembl
    10. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731A → V in AO1. 1 Publication
    Corresponds to variant rs28937586 [ dbSNP | Ensembl ].
    VAR_033072
    Natural varianti188 – 1881S → P in AO1. 1 Publication
    VAR_033073
    Natural varianti202 – 2021M → V in AO1 and AO3. 1 Publication
    Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
    VAR_033074
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti202 – 2021M → V in AO1 and AO3. 1 Publication
    Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
    VAR_033074
    Natural varianti751 – 7511G → R in AO3. 1 Publication
    Corresponds to variant rs28937587 [ dbSNP | Ensembl ].
    VAR_033080
    Boomerang dysplasia (BOOMD) [MIM:112310]: A perinatal lethal osteochondrodysplasia characterized by absence or underossification of the limb bones and vertebrae. Patients manifest dwarfism with short, bowed, rigid limbs and characteristic facies. Boomerang dysplasia is distinguished from atelosteogenesis on the basis of a more severe defect in mineralization, with complete absence of ossification in some limb elements and vertebral segments.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711L → R in BOOMD. 1 Publication
    VAR_033071
    Natural varianti235 – 2351S → P in BOOMD. 1 Publication
    VAR_033077
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti161 – 1611F → C in LRS. 2 Publications
    VAR_033069
    Natural varianti168 – 1681G → S in LRS. 1 Publication
    VAR_033070
    Natural varianti227 – 2271E → K in LRS. 2 Publications
    VAR_033075
    Natural varianti234 – 2341L → V in LRS. 1 Publication
    VAR_033076
    Natural varianti361 – 3611G → S in LRS. 1 Publication
    VAR_033078
    Natural varianti363 – 3631G → E in LRS. 1 Publication
    VAR_033079
    Natural varianti1431 – 14311L → R in LRS. 1 Publication
    VAR_033081
    Natural varianti1571 – 15711Missing in LRS. 2 Publications
    VAR_033082
    Natural varianti1586 – 15861G → R in LRS. 2 Publications
    Corresponds to variant rs28939706 [ dbSNP | Ensembl ].
    VAR_033083
    Natural varianti1592 – 15921V → D in LRS. 1 Publication
    VAR_033084
    Natural varianti1603 – 16031P → L in LRS. 1 Publication
    VAR_033085
    Natural varianti1691 – 16911G → S in LRS. 2 Publications
    VAR_033086
    Natural varianti1834 – 18341G → R in LRS. 1 Publication
    VAR_033087
    Spondylocarpotarsal synostosis syndrome (SCT) [MIM:272460]: Disorder characterized by short stature and vertebral, carpal and tarsal fusions.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2468 – 24681K → R: Cytoplasmic localization. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi108720. phenotype.
    108721. phenotype.
    112310. phenotype.
    150250. phenotype.
    272460. phenotype.
    Orphaneti1190. Atelosteogenesis type I.
    56305. Atelosteogenesis type III.
    503. Autosomal dominant Larsen syndrome.
    1263. Boomerang dysplasia.
    3275. Spondylocarpotarsal synostosis.
    PharmGKBiPA28173.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 26022602Filamin-BPRO_0000087298Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei519 – 5191Phosphothreonine2 Publications
    Modified residuei681 – 6811N6-acetyllysine1 Publication
    Modified residuei730 – 7301Phosphoserine1 Publication
    Modified residuei886 – 8861Phosphoserine1 Publication
    Modified residuei932 – 9321Phosphoserine1 Publication
    Modified residuei983 – 9831Phosphoserine4 Publications
    Modified residuei1028 – 10281Phosphoserine1 Publication
    Modified residuei1316 – 13161Phosphoserine2 Publications
    Modified residuei1433 – 14331Phosphoserine1 Publication
    Modified residuei1505 – 15051Phosphoserine1 Publication
    Modified residuei1602 – 16021Phosphoserine1 Publication
    Modified residuei1780 – 17801N6-acetyllysineBy similarity
    Modified residuei2083 – 20831Phosphoserine1 Publication
    Modified residuei2107 – 21071Phosphoserine1 Publication
    Modified residuei2369 – 23691Phosphoserine1 Publication
    Modified residuei2465 – 24651Phosphoserine1 Publication
    Cross-linki2468 – 2468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
    Modified residuei2478 – 24781Phosphoserine3 Publications
    Modified residuei2481 – 24811Phosphoserine1 Publication
    Modified residuei2518 – 25181N6-succinyllysineBy similarity
    Modified residuei2524 – 25241N6-succinyllysineBy similarity
    Modified residuei2576 – 25761N6-acetyllysine1 Publication

    Post-translational modificationi

    ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO75369.
    PaxDbiO75369.
    PRIDEiO75369.

    PTM databases

    PhosphoSiteiO75369.

    Expressioni

    Tissue specificityi

    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.4 Publications

    Gene expression databases

    ArrayExpressiO75369.
    BgeeiO75369.
    GenevestigatoriO75369.

    Organism-specific databases

    HPAiCAB019322.
    HPA004747.
    HPA004886.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with MICALL2 By similarity. 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.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-352089,EBI-352089
    FLNAP213335EBI-352089,EBI-350432
    GRB2P629932EBI-352089,EBI-401755
    ISG15P051614EBI-352089,EBI-746466
    MAP3K1Q132332EBI-352089,EBI-49776
    MAP3K4Q9Y6R42EBI-352089,EBI-448104
    NCK1P163333EBI-352089,EBI-389883
    RAC1P630002EBI-352089,EBI-413628

    Protein-protein interaction databases

    BioGridi108606. 54 interactions.
    IntActiO75369. 29 interactions.
    MINTiMINT-4998813.

    Structurei

    Secondary structure

    1
    2602
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 106
    Helixi13 – 164
    Helixi17 – 3014
    Helixi31 – 333
    Turni40 – 467
    Helixi48 – 5811
    Helixi73 – 8917
    Helixi99 – 1035
    Helixi107 – 12216
    Helixi141 – 15212
    Helixi163 – 1653
    Helixi169 – 17810
    Helixi186 – 1883
    Helixi194 – 20815
    Helixi217 – 2204
    Helixi227 – 2348
    Helixi236 – 2394
    Helixi254 – 2563
    Beta strandi258 – 2614
    Helixi262 – 2643
    Beta strandi265 – 2673
    Beta strandi275 – 2806
    Turni282 – 2843
    Beta strandi289 – 2946
    Beta strandi300 – 3023
    Beta strandi304 – 3096
    Beta strandi313 – 3197
    Beta strandi323 – 33311
    Beta strandi342 – 3476
    Helixi1040 – 10423
    Beta strandi1044 – 10474
    Helixi1048 – 10514
    Beta strandi1052 – 10543
    Beta strandi1059 – 10646
    Turni1066 – 10683
    Beta strandi1073 – 10775
    Beta strandi1079 – 10813
    Beta strandi1084 – 10896
    Beta strandi1091 – 110010
    Beta strandi1102 – 111514
    Beta strandi1122 – 11287
    Helixi1133 – 11353
    Beta strandi1136 – 11405
    Helixi1141 – 11433
    Beta strandi1154 – 11607
    Beta strandi1166 – 11727
    Turni1173 – 11753
    Beta strandi1179 – 11846
    Beta strandi1188 – 11958
    Beta strandi1200 – 12089
    Beta strandi1217 – 12237
    Beta strandi1232 – 12354
    Helixi1236 – 12394
    Beta strandi1249 – 12546
    Beta strandi1256 – 12583
    Beta strandi1273 – 12753
    Beta strandi1281 – 12844
    Beta strandi1286 – 12949
    Beta strandi1300 – 131011
    Beta strandi1317 – 13215
    Beta strandi1332 – 13354
    Helixi1336 – 13394
    Beta strandi1347 – 13526
    Turni1354 – 13563
    Beta strandi1361 – 13699
    Beta strandi1374 – 13774
    Beta strandi1379 – 13813
    Beta strandi1383 – 13875
    Beta strandi1393 – 14019
    Beta strandi1410 – 14167
    Beta strandi1425 – 14284
    Turni1429 – 14313
    Beta strandi1441 – 14466
    Turni1448 – 14503
    Beta strandi1455 – 14606
    Beta strandi1462 – 14643
    Beta strandi1475 – 14839
    Beta strandi1489 – 150113
    Beta strandi1506 – 15127
    Helixi1517 – 15193
    Beta strandi1520 – 15245
    Helixi1525 – 15273
    Beta strandi1538 – 15469
    Beta strandi1566 – 15705
    Beta strandi1573 – 15808
    Beta strandi1586 – 15905
    Beta strandi1593 – 15964
    Beta strandi1603 – 16097
    Beta strandi1618 – 16214
    Helixi1622 – 16243
    Beta strandi1625 – 163915
    Beta strandi1641 – 16433
    Beta strandi1648 – 16536
    Beta strandi1663 – 16664
    Beta strandi1672 – 16776
    Beta strandi1682 – 169211
    Beta strandi1699 – 17057
    Beta strandi1748 – 17503
    Beta strandi1759 – 17657
    Beta strandi1775 – 17784
    Beta strandi1780 – 17823
    Beta strandi1784 – 17874
    Beta strandi1792 – 180413
    Beta strandi1811 – 18166
    Beta strandi1825 – 18284
    Helixi1829 – 18324
    Beta strandi1833 – 18353
    Beta strandi1840 – 18456
    Beta strandi1854 – 18629
    Beta strandi1872 – 188110
    Beta strandi1888 – 189811
    Beta strandi1903 – 19097
    Beta strandi1924 – 19274
    Beta strandi1941 – 19433
    Beta strandi1952 – 19576
    Turni1958 – 19603
    Beta strandi1961 – 19666
    Beta strandi1972 – 19776
    Beta strandi1979 – 19846
    Beta strandi1989 – 19946
    Beta strandi1997 – 19993
    Helixi2002 – 20043
    Beta strandi2006 – 20105
    Turni2011 – 20133
    Beta strandi2014 – 20163
    Beta strandi2021 – 20266
    Turni2028 – 20303
    Beta strandi2035 – 20439
    Beta strandi2057 – 20615
    Beta strandi2067 – 207711
    Beta strandi2084 – 20907
    Beta strandi2111 – 21133
    Beta strandi2118 – 21203
    Helixi2126 – 21283
    Beta strandi2130 – 21345
    Beta strandi2140 – 21423
    Beta strandi2144 – 21474
    Beta strandi2149 – 21579
    Beta strandi2164 – 217512
    Beta strandi2180 – 21856
    Helixi2193 – 21953
    Turni2201 – 22033
    Beta strandi2206 – 22083
    Beta strandi2210 – 22145
    Beta strandi2219 – 22213
    Beta strandi2226 – 22349
    Beta strandi2236 – 22405
    Beta strandi2250 – 22567
    Beta strandi2258 – 22669
    Beta strandi2275 – 22817
    Beta strandi2288 – 22947
    Beta strandi2306 – 23149
    Beta strandi2320 – 23245
    Beta strandi2330 – 23323
    Beta strandi2334 – 23374
    Beta strandi2340 – 23478
    Beta strandi2352 – 236514
    Beta strandi2370 – 23756
    Turni2384 – 23863
    Beta strandi2388 – 23925
    Turni2393 – 23953
    Beta strandi2403 – 24086
    Turni2410 – 24123
    Beta strandi2417 – 24259
    Beta strandi2430 – 24334
    Beta strandi2435 – 24428
    Beta strandi2448 – 245912
    Beta strandi2466 – 24738
    Turni2512 – 25143
    Beta strandi2516 – 25194
    Helixi2520 – 25234
    Beta strandi2531 – 25366
    Turni2538 – 25403
    Beta strandi2545 – 25473
    Beta strandi2557 – 25659
    Beta strandi2568 – 25747
    Beta strandi2579 – 25835
    Beta strandi2585 – 25917
    Beta strandi2596 – 26016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO75369.
    SMRiO75369. Positions 13-347, 450-739, 1017-1723, 1735-2488, 2511-2602.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75369.

    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
    Regioni1128 – 1511384Interaction with FBLP1Add
    BLAST
    Regioni1705 – 172824Hinge 1By similarityAdd
    BLAST
    Regioni1862 – 2148287Interaction with the cytoplasmic tail of GP1BAAdd
    BLAST
    Regioni2060 – 2225166Interaction with FLNA 1Add
    BLAST
    Regioni2130 – 2602473Interaction with INPPL1Add
    BLAST
    Regioni2472 – 2602131Self-association site, tailBy similarityAdd
    BLAST
    Regioni2472 – 250635Hinge 2By similarityAdd
    BLAST
    Regioni2507 – 260296Interaction with FLNA 2Add
    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.

    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

    eggNOGiCOG5069.
    HOGENOMiHOG000044235.
    HOVERGENiHBG004163.
    InParanoidiO75369.
    KOiK04437.
    OMAiDQEGKPK.
    OrthoDBiEOG76T9QC.
    PhylomeDBiO75369.
    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.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view]
    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]

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75369-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL     50
    IALLEVLSQK RMYRKYHQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK 100
    AIVDGNLKLI LGLVWTLILH YSISMPVWED EGDDDAKKQT PKQRLLGWIQ 150
    NKIPYLPITN FNQNWQDGKA LGALVDSCAP GLCPDWESWD PQKPVDNARE 200
    AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA KLKPGAPLKP 250
    KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK 300
    EEAQVTPDSD KNKTYSVEYL PKVTGLHKVT VLFAGQHISK SPFEVSVDKA 350
    QGDASKVTAK GPGLEAVGNI ANKPTYFDIY TAGAGVGDIG VEVEDPQGKN 400
    TVELLVEDKG NQVYRCVYKP MQPGPHVVKI FFAGDTIPKS PFVVQVGEAC 450
    NPNACRASGR GLQPKGVRIR ETTDFKVDTK AAGSGELGVT MKGPKGLEEL 500
    VKQKDFLDGV YAFEYYPSTP GRYSIAITWG GHHIPKSPFE VQVGPEAGMQ 550
    KVRAWGPGLH GGIVGRSADF VVESIGSEVG SLGFAIEGPS QAKIEYNDQN 600
    DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GGYNPDLVRA 650
    YGPGLEKSGC IVNNLAEFTV DPKDAGKAPL KIFAQDGEGQ RIDIQMKNRM 700
    DGTYACSYTP VKAIKHTIAV VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP 750
    GVERSGLKAN EPTHFTVDCT EAGEGDVSVG IKCDARVLSE DEEDVDFDII 800
    HNANDTFTVK YVPPAAGRYT IKVLFASQEI PASPFRVKVD PSHDASKVKA 850
    EGPGLSKAGV ENGKPTHFTV YTKGAGKAPL NVQFNSPLPG DAVKDLDIID 900
    NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKLN 950
    GLENRVEVGK DQEFTVDTRG AGGQGKLDVT ILSPSRKVVP CLVTPVTGRE 1000
    NSTAKFIPRE EGLYAVDVTY DGHPVPGSPY TVEASLPPDP SKVKAHGPGL 1050
    EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP CEAKIECSDN GDGTCSVSYL 1100
    PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG PGLEHGKVGE 1150
    AGLLSVDCSE AGPGALGLEA VSDSGTKAEV SIQNNKDGTY AVTYVPLTAG 1200
    MYTLTMKYGG ELVPHFPARV KVEPAVDTSR IKVFGPGIEG KDVFREATTD 1250
    FTVDSRPLTQ VGGDHIKAHI ANPSGASTEC FVTDNADGTY QVEYTPFEKG 1300
    LHVVEVTYDD VPIPNSPFKV AVTEGCQPSR VQAQGPGLKE AFTNKPNVFT 1350
    VVTRGAGIGG LGITVEGPSE SKINCRDNKD GSCSAEYIPF APGDYDVNIT 1400
    YGGAHIPGSP FRVPVKDVVD PSKVKIAGPG LGSGVRARVL QSFTVDSSKA 1450
    GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YMVSVKYADE 1500
    EIPRSPFKVK VLPTYDASKV TASGPGLSSY GVPASLPVDF AIDARDAGEG 1550
    LLAVQITDQE GKPKRAIVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDDIP 1600
    LSPYRIRATQ TGDASKCLAT GPGIASTVKT GEEVGFVVDA KTAGKGKVTC 1650
    TVLTPDGTEA EADVIENEDG TYDIFYTAAK PGTYVIYVRF GGVDIPNSPF 1700
    TVMATDGEVT AVEEAPVNAC PPGFRPWVTE EAYVPVSDMN GLGFKPFDLV 1750
    IPFAVRKGEI TGEVHMPSGK TATPEIVDNK DGTVTVRYAP TEVGLHEMHI 1800
    KYMGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG 1850
    EGGLDLAIEG PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP 1900
    GSPFTAKITD DSRRCSQVKL GSAADFLLDI SETDLSSLTA SIKAPSGRDE 1950
    PCLLKRLPNN HIGISFIPRE VGEHLVSIKK NGNHVANSPV SIMVVQSEIG 2000
    DARRAKVYGR GLSEGRTFEM SDFIVDTRDA GYGGISLAVE GPSKVDIQTE 2050
    DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVKESIT 2100
    RTSRAPSVAT VGSICDLNLK IPEINSSDMS AHVTSPSGRV TEAEIVPMGK 2150
    NSHCVRFVPQ EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG 2200
    PGLERGEAGV PAEFSIWTRE AGAGGLSIAV EGPSKAEITF DDHKNGSCGV 2250
    SYIAQEPGNY EVSIKFNDEH IPESPYLVPV IAPSDDARRL TVMSLQESGL 2300
    KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP DKYAVRFIPH 2350
    ENGVHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GTGLEGGTTG 2400
    IQSEFFINTT RAGPGTLSVT IEGPSKVKMD CQETPEGYKV MYTPMAPGNY 2450
    LISVKYGGPN HIVGSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET 2500
    CYSAIPKASS DASKVTSKGA GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH 2550
    GPTTPCEEVS MKHVGNQQYN VTYVVKERGD YVLAVKWGEE HIPGSPFHVT 2600
    VP 2602
    Length:2,602
    Mass (Da):278,164
    Last modified:May 18, 2010 - v2
    Checksum:i1BF5C64C86360C6A
    GO
    Isoform 2 (identifier: O75369-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:2,578
    Mass (Da):275,668
    Checksum:i4E51115028A676F8
    GO
    Isoform 3 (identifier: O75369-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:2,561
    Mass (Da):273,909
    Checksum:iA367021E1BCF1EF1
    GO
    Isoform 7 (identifier: O75369-7) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,422
    Mass (Da):257,551
    Checksum:i8BB43D0D58E153B1
    GO
    Isoform 4 (identifier: O75369-4) [UniParc]FASTAAdd to Basket

    Also known as: Var-3

    The sequence of this isoform differs from the canonical sequence as follows:
         2123-2150: EINSSDMSAHVTSPSGRVTEAEIVPMGK → GVRVMNCSAQILWGWRVQFHTGSRNQQQ
         2151-2602: Missing.

    Show »
    Length:2,150
    Mass (Da):230,788
    Checksum:iB1FDAE6F0E99947C
    GO
    Isoform 5 (identifier: O75369-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:2,146
    Mass (Da):230,289
    Checksum:i0E99947C9734D59E
    GO
    Isoform 6 (identifier: O75369-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:2,537
    Mass (Da):271,413
    Checksum:iDABD7554C44F38DA
    GO
    Isoform 8 (identifier: O75369-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1463-1463: R → RADDTDSQSWRSPLKALSEFFKGDPKGDFNKT

    Show »
    Length:2,633
    Mass (Da):281,635
    Checksum:i8D8F7817049EECA1
    GO
    Isoform 9 (identifier: O75369-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1717-1727: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,591
    Mass (Da):276,939
    Checksum:i2D9AF6AF4D1469EF
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti816 – 8161A → T in CAE46040. (PubMed:17974005)Curated
    Sequence conflicti924 – 9241Y → H in CAE46040. (PubMed:17974005)Curated
    Sequence conflicti1411 – 14111F → L in CAE46040. (PubMed:17974005)Curated
    Sequence conflicti1560 – 15601E → G in CAE46040. (PubMed:17974005)Curated
    Sequence conflicti1953 – 19531L → F in AAF97046. (PubMed:11153914)Curated
    Sequence conflicti2006 – 20061K → R in AAC33845. (PubMed:9694715)Curated
    Sequence conflicti2099 – 20991I → S in CAE46040. (PubMed:17974005)Curated
    Sequence conflicti2170 – 21701K → N in AAF97046. (PubMed:11153914)Curated
    Sequence conflicti2293 – 22931M → V in AAF97046. (PubMed:11153914)Curated
    Sequence conflicti2293 – 22931M → V in CAE46040. (PubMed:17974005)Curated
    Sequence conflicti2354 – 23541V → A in CAB70818. (PubMed:11230166)Curated
    Sequence conflicti2487 – 24871S → C in AAA35505. (PubMed:8327473)Curated
    Sequence conflicti2571 – 25711V → A in CAB70818. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti161 – 1611F → C in LRS. 2 Publications
    VAR_033069
    Natural varianti168 – 1681G → S in LRS. 1 Publication
    VAR_033070
    Natural varianti171 – 1711L → R in BOOMD. 1 Publication
    VAR_033071
    Natural varianti173 – 1731A → V in AO1. 1 Publication
    Corresponds to variant rs28937586 [ dbSNP | Ensembl ].
    VAR_033072
    Natural varianti188 – 1881S → P in AO1. 1 Publication
    VAR_033073
    Natural varianti202 – 2021M → V in AO1 and AO3. 1 Publication
    Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
    VAR_033074
    Natural varianti227 – 2271E → K in LRS. 2 Publications
    VAR_033075
    Natural varianti234 – 2341L → V in LRS. 1 Publication
    VAR_033076
    Natural varianti235 – 2351S → P in BOOMD. 1 Publication
    VAR_033077
    Natural varianti361 – 3611G → S in LRS. 1 Publication
    VAR_033078
    Natural varianti363 – 3631G → E in LRS. 1 Publication
    VAR_033079
    Natural varianti566 – 5661R → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035917
    Natural varianti663 – 6631N → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035918
    Natural varianti703 – 7031T → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035919
    Natural varianti751 – 7511G → R in AO3. 1 Publication
    Corresponds to variant rs28937587 [ dbSNP | Ensembl ].
    VAR_033080
    Natural varianti1018 – 10181V → M.
    Corresponds to variant rs2276742 [ dbSNP | Ensembl ].
    VAR_017182
    Natural varianti1157 – 11571D → N.3 Publications
    Corresponds to variant rs1131356 [ dbSNP | Ensembl ].
    VAR_017183
    Natural varianti1179 – 11791E → K.
    Corresponds to variant rs17058845 [ dbSNP | Ensembl ].
    VAR_031392
    Natural varianti1431 – 14311L → R in LRS. 1 Publication
    VAR_033081
    Natural varianti1471 – 14711V → M.3 Publications
    Corresponds to variant rs12632456 [ dbSNP | Ensembl ].
    VAR_031393
    Natural varianti1534 – 15341A → G in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035920
    Natural varianti1571 – 15711Missing in LRS. 2 Publications
    VAR_033082
    Natural varianti1586 – 15861G → R in LRS. 2 Publications
    Corresponds to variant rs28939706 [ dbSNP | Ensembl ].
    VAR_033083
    Natural varianti1592 – 15921V → D in LRS. 1 Publication
    VAR_033084
    Natural varianti1603 – 16031P → L in LRS. 1 Publication
    VAR_033085
    Natural varianti1691 – 16911G → S in LRS. 2 Publications
    VAR_033086
    Natural varianti1834 – 18341G → R in LRS. 1 Publication
    VAR_033087

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 169169Missing in isoform 7. 1 PublicationVSP_024113Add
    BLAST
    Alternative sequencei170 – 18112ALGAL…SCAPG → MQEHSTRRRSLS in isoform 7. 1 PublicationVSP_024114Add
    BLAST
    Alternative sequencei1463 – 14631R → RADDTDSQSWRSPLKALSEF FKGDPKGDFNKT in isoform 8. 2 PublicationsVSP_043446
    Alternative sequencei1704 – 172724Missing in isoform 2 and isoform 6. 3 PublicationsVSP_008773Add
    BLAST
    Alternative sequencei1717 – 172711Missing in isoform 7 and isoform 9. 3 PublicationsVSP_024115Add
    BLAST
    Alternative sequencei2081 – 212141Missing in isoform 3 and isoform 6. CuratedVSP_008774Add
    BLAST
    Alternative sequencei2123 – 215028EINSS…VPMGK → GVRVMNCSAQILWGWRVQFH TGSRNQQQ in isoform 4. CuratedVSP_008775Add
    BLAST
    Alternative sequencei2123 – 214624EINSS…EAEIV → GVRVMNCSAQILWGWRVQFH TGSR in isoform 5. CuratedVSP_008777Add
    BLAST
    Alternative sequencei2147 – 2602456Missing in isoform 5. CuratedVSP_008778Add
    BLAST
    Alternative sequencei2151 – 2602452Missing in isoform 4. CuratedVSP_008776Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS2885.1. [O75369-1]
    CCDS54599.1. [O75369-8]
    CCDS54600.1. [O75369-9]
    CCDS54601.1. [O75369-2]
    PIRiT46270.
    RefSeqiNP_001157789.1. NM_001164317.1. [O75369-8]
    NP_001157790.1. NM_001164318.1. [O75369-9]
    NP_001157791.1. NM_001164319.1. [O75369-2]
    NP_001448.2. NM_001457.3. [O75369-1]
    UniGeneiHs.476448.

    Genome annotation databases

    EnsembliENST00000295956; ENSP00000295956; ENSG00000136068. [O75369-1]
    ENST00000358537; ENSP00000351339; ENSG00000136068. [O75369-2]
    ENST00000419752; ENSP00000414532; ENSG00000136068. [O75369-7]
    ENST00000429972; ENSP00000415599; ENSG00000136068. [O75369-9]
    ENST00000490882; ENSP00000420213; ENSG00000136068. [O75369-8]
    GeneIDi2317.
    KEGGihsa:2317.
    UCSCiuc003djj.2. human. [O75369-1]
    uc003djk.2. human. [O75369-9]
    uc003djl.2. human. [O75369-7]
    uc010hne.2. human. [O75369-8]
    uc010hnf.2. human. [O75369-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSi CCDS2885.1. [O75369-1 ]
    CCDS54599.1. [O75369-8 ]
    CCDS54600.1. [O75369-9 ]
    CCDS54601.1. [O75369-2 ]
    PIRi T46270.
    RefSeqi NP_001157789.1. NM_001164317.1. [O75369-8 ]
    NP_001157790.1. NM_001164318.1. [O75369-9 ]
    NP_001157791.1. NM_001164319.1. [O75369-2 ]
    NP_001448.2. NM_001457.3. [O75369-1 ]
    UniGenei Hs.476448.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DI8 NMR - A 1999-2096 [» ]
    2DI9 NMR - A 1017-1134 [» ]
    2DIA NMR - A 1130-1229 [» ]
    2DIB NMR - A 1215-1329 [» ]
    2DIC NMR - A 1325-1422 [» ]
    2DJ4 NMR - A 1418-1518 [» ]
    2DLG NMR - A 2104-2192 [» ]
    2DMB NMR - A 1611-1721 [» ]
    2DMC NMR - A 1899-2001 [» ]
    2E9I NMR - A 2094-2192 [» ]
    2E9J NMR - A 1504-1615 [» ]
    2EE6 NMR - A 2190-2287 [» ]
    2EE9 NMR - A 1736-1823 [» ]
    2EEA NMR - A 1808-1915 [» ]
    2EEB NMR - A 2284-2382 [» ]
    2EEC NMR - A 2371-2488 [» ]
    2EED NMR - A 2509-2602 [» ]
    2WA5 X-ray 1.90 A 2-242 [» ]
    2WA6 X-ray 1.95 A 2-242 [» ]
    2WA7 X-ray 1.85 A 2-242 [» ]
    3FER X-ray 2.40 A/B/C/D 1-252 [» ]
    4B7L X-ray 2.05 A/B 1-347 [» ]
    ProteinModelPortali O75369.
    SMRi O75369. Positions 13-347, 450-739, 1017-1723, 1735-2488, 2511-2602.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108606. 54 interactions.
    IntActi O75369. 29 interactions.
    MINTi MINT-4998813.

    PTM databases

    PhosphoSitei O75369.

    Proteomic databases

    MaxQBi O75369.
    PaxDbi O75369.
    PRIDEi O75369.

    Protocols and materials databases

    DNASUi 2317.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295956 ; ENSP00000295956 ; ENSG00000136068 . [O75369-1 ]
    ENST00000358537 ; ENSP00000351339 ; ENSG00000136068 . [O75369-2 ]
    ENST00000419752 ; ENSP00000414532 ; ENSG00000136068 . [O75369-7 ]
    ENST00000429972 ; ENSP00000415599 ; ENSG00000136068 . [O75369-9 ]
    ENST00000490882 ; ENSP00000420213 ; ENSG00000136068 . [O75369-8 ]
    GeneIDi 2317.
    KEGGi hsa:2317.
    UCSCi uc003djj.2. human. [O75369-1 ]
    uc003djk.2. human. [O75369-9 ]
    uc003djl.2. human. [O75369-7 ]
    uc010hne.2. human. [O75369-8 ]
    uc010hnf.2. human. [O75369-2 ]

    Organism-specific databases

    CTDi 2317.
    GeneCardsi GC03P057969.
    GeneReviewsi FLNB.
    H-InvDB HIX0003397.
    HGNCi HGNC:3755. FLNB.
    HPAi CAB019322.
    HPA004747.
    HPA004886.
    MIMi 108720. phenotype.
    108721. phenotype.
    112310. phenotype.
    150250. phenotype.
    272460. phenotype.
    603381. gene.
    neXtProti NX_O75369.
    Orphaneti 1190. Atelosteogenesis type I.
    56305. Atelosteogenesis type III.
    503. Autosomal dominant Larsen syndrome.
    1263. Boomerang dysplasia.
    3275. Spondylocarpotarsal synostosis.
    PharmGKBi PA28173.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000044235.
    HOVERGENi HBG004163.
    InParanoidi O75369.
    KOi K04437.
    OMAi DQEGKPK.
    OrthoDBi EOG76T9QC.
    PhylomeDBi O75369.
    TreeFami TF313685.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    SignaLinki O75369.

    Miscellaneous databases

    ChiTaRSi FLNB. human.
    EvolutionaryTracei O75369.
    GeneWikii FLNB.
    GenomeRNAii 2317.
    NextBioi 9409.
    PROi O75369.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75369.
    Bgeei O75369.
    Genevestigatori O75369.

    Family and domain databases

    Gene3Di 1.10.418.10. 2 hits.
    2.60.40.10. 24 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR017868. Filamin/ABP280_repeat-like.
    IPR001298. Filamin/ABP280_rpt.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF00630. Filamin. 23 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00557. IG_FLMN. 24 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF81296. SSF81296. 24 hits.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS50194. FILAMIN_REPEAT. 24 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. Cited for: REVIEW.
    20. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "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.
    32. "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.
    33. 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.
    34. "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.
    35. Cited for: VARIANTS BOOMD ARG-171 AND PRO-235.
    36. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-566; LYS-663; LYS-703 AND GLY-1534.
    37. 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.

    Entry informationi

    Entry nameiFLNB_HUMAN
    AccessioniPrimary (citable) accession number: O75369
    Secondary accession number(s): B2ZZ83
    , B2ZZ84, B2ZZ85, C9JKE6, C9JMC4, Q13706, Q59EC2, Q60FE7, Q6MZJ1, Q8WXS9, Q8WXT0, Q8WXT1, Q8WXT2, Q9NRB5, Q9NT26, Q9UEV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3