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P21333

- FLNA_HUMAN

UniProt

P21333 - FLNA_HUMAN

Protein

Filamin-A

Gene

FLNA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking By similarity. Involved in ciliogenesis.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1761 – 17622Cleavage; by calpain

    GO - Molecular functioni

    1. actin filament binding Source: BHF-UCL
    2. Fc-gamma receptor I complex binding Source: BHF-UCL
    3. glycoprotein binding Source: BHF-UCL
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: BHF-UCL
    7. Rac GTPase binding Source: BHF-UCL
    8. Ral GTPase binding Source: BHF-UCL
    9. Rho GTPase binding Source: BHF-UCL
    10. signal transducer activity Source: UniProtKB
    11. small GTPase binding Source: BHF-UCL
    12. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. actin crosslink formation Source: BHF-UCL
    2. actin cytoskeleton reorganization Source: BHF-UCL
    3. adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: BHF-UCL
    4. blood coagulation Source: Reactome
    5. cell junction assembly Source: Reactome
    6. cilium assembly Source: UniProtKB
    7. cytoplasmic sequestering of protein Source: BHF-UCL
    8. early endosome to late endosome transport Source: Ensembl
    9. epithelial to mesenchymal transition Source: Ensembl
    10. establishment of protein localization Source: BHF-UCL
    11. mRNA transcription from RNA polymerase II promoter Source: Ensembl
    12. negative regulation of protein catabolic process Source: BHF-UCL
    13. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    14. platelet activation Source: Reactome
    15. platelet degranulation Source: Reactome
    16. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    17. positive regulation of transcription factor import into nucleus Source: UniProtKB
    18. protein localization to cell surface Source: BHF-UCL
    19. protein stabilization Source: BHF-UCL
    20. receptor clustering Source: BHF-UCL
    21. spindle assembly involved in mitosis Source: MGI

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_20649. Cell-extracellular matrix interactions.
    REACT_23847. GP1b-IX-V activation signalling.
    SignaLinkiP21333.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Filamin-A
    Short name:
    FLN-A
    Alternative name(s):
    Actin-binding protein 280
    Short name:
    ABP-280
    Alpha-filamin
    Endothelial actin-binding protein
    Filamin-1
    Non-muscle filamin
    Gene namesi
    Name:FLNA
    Synonyms:FLN, FLN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3754. FLNA.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: BHF-UCL
    2. actin filament Source: Ensembl
    3. apical dendrite Source: Ensembl
    4. cortical cytoskeleton Source: Ensembl
    5. cytoplasm Source: UniProtKB
    6. cytosol Source: Reactome
    7. dendritic shaft Source: Ensembl
    8. extracellular region Source: Reactome
    9. extracellular vesicular exosome Source: UniProtKB
    10. membrane Source: UniProtKB
    11. Myb complex Source: MGI
    12. neuronal cell body Source: Ensembl
    13. nucleus Source: UniProtKB
    14. perinuclear region of cytoplasm Source: Ensembl
    15. plasma membrane Source: BHF-UCL
    16. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Periventricular nodular heterotopia 1 (PVNH1) [MIM:300049]: A developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821E → V in PVNH1. 1 Publication
    Corresponds to variant rs28935169 [ dbSNP | Ensembl ].
    VAR_015699
    Natural varianti102 – 1021M → V in PVNH1. 1 Publication
    VAR_031305
    Natural varianti149 – 1491S → F in PVNH1. 1 Publication
    VAR_031307
    Natural varianti528 – 5281V → M in PVNH1. 1 Publication
    Corresponds to variant rs143873938 [ dbSNP | Ensembl ].
    VAR_031309
    Natural varianti656 – 6561L → F in PVNH1. 1 Publication
    VAR_012834
    Periventricular nodular heterotopia 4 (PVNH4) [MIM:300537]: A disorder characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391A → G in PVNH4. 1 Publication
    VAR_022734
    Natural varianti128 – 1281A → V in PVNH4. 1 Publication
    VAR_031306
    Otopalatodigital syndrome 1 (OPD1) [MIM:311300]: X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721L → F in OPD1. 1 Publication
    VAR_015714
    Natural varianti196 – 1961R → W in OPD1. 1 Publication
    VAR_015716
    Natural varianti203 – 2031D → Y in OPD1. 1 Publication
    VAR_031308
    Natural varianti207 – 2071P → L in OPD1. 1 Publication
    Corresponds to variant rs28935469 [ dbSNP | Ensembl ].
    VAR_015700
    Otopalatodigital syndrome 2 (OPD2) [MIM:304120]: Congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1701Q → P in OPD2. 1 Publication
    VAR_015713
    Natural varianti196 – 1961R → G in OPD2. 1 Publication
    VAR_015715
    Natural varianti200 – 2001A → S in OPD2. 1 Publication
    VAR_015717
    Natural varianti210 – 2101C → F in OPD2. 1 Publication
    VAR_058720
    Natural varianti254 – 2541E → K in OPD2. 1 Publication
    Corresponds to variant rs28935470 [ dbSNP | Ensembl ].
    VAR_015701
    Natural varianti273 – 2731A → P in OPD2. 1 Publication
    VAR_015718
    Natural varianti555 – 5551T → K in OPD2. 1 Publication
    VAR_015719
    Natural varianti1645 – 16451C → F in OPD2. 1 Publication
    VAR_015723
    Frontometaphyseal dysplasia (FMD) [MIM:305620]: Congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1159 – 11591D → A in FMD; does not inhibit interaction with MIS18BP1. 1 Publication
    Corresponds to variant rs28935471 [ dbSNP | Ensembl ].
    VAR_015702
    Natural varianti1186 – 11861S → L in FMD. 2 Publications
    VAR_015721
    Natural varianti1620 – 16201Missing in FMD. 1 Publication
    VAR_015722
    Natural varianti1728 – 17281G → C in FMD. 1 Publication
    VAR_031312
    Melnick-Needles syndrome (MNS) [MIM:309350]: Severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1184 – 11841D → E in MNS. 1 Publication
    VAR_015720
    Natural varianti1188 – 11881A → T in MNS; does not inhibit interaction with MIS18BP1. 1 Publication
    Corresponds to variant rs28935472 [ dbSNP | Ensembl ].
    VAR_015703
    Natural varianti1199 – 11991S → L in MNS; does not inhibit interaction with MIS18BP1. 1 Publication
    Corresponds to variant rs28935473 [ dbSNP | Ensembl ].
    VAR_015704
    Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-linked (IPOX) [MIM:300048]: A disease characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1291 – 12911P → L in FGS2. 1 Publication
    VAR_058721
    Terminal osseous dysplasia (TOD) [MIM:300244]: A rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1724 – 173916Missing in TOD. 1 Publication
    VAR_064159Add
    BLAST
    Cardiac valvular dysplasia X-linked (CVDX) [MIM:314400]: A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti288 – 2881G → R in CVDX. 1 Publication
    VAR_064156
    Natural varianti637 – 6371P → Q in CVDX. 1 Publication
    VAR_064157
    Natural varianti711 – 7111V → D in CVDX. 1 Publication
    VAR_064158
    Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abnormally enlarged.
    Congenital short bowel syndrome, X-linked (CSBSX) [MIM:300048]: A disease characterized by a shortened small intestine, and malabsorption. The mean length of the small intestine in affected individuals is approximately 50 cm, compared with a normal length at birth of 190-280 cm. It is associated with significant mortality and morbidity. Infants usually present with failure to thrive, recurrent vomiting, and diarrhea.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi300048. phenotype.
    300049. phenotype.
    300244. phenotype.
    300321. phenotype.
    300537. phenotype.
    304120. phenotype.
    305620. phenotype.
    309350. phenotype.
    311300. phenotype.
    314400. phenotype.
    Orphaneti2978. Chronic intestinal pseudoobstruction.
    2301. Congenital short bowel syndrome.
    1864. Congenital valvular dysplasia.
    82004. Ehlers-Danlos syndrome with periventricular heterotopia.
    323. FG syndrome.
    1826. Frontometaphyseal dysplasia.
    2484. Osteodysplasty, Melnick-Needles type.
    90650. Otopalatodigital syndrome type 1.
    90652. Otopalatodigital syndrome type 2.
    98892. Periventricular nodular heterotopia.
    88630. Terminal osseous dysplasia - pigmentary defects.
    PharmGKBiPA28172.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 26472646Filamin-APRO_0000087296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei11 – 111Phosphoserine1 Publication
    Modified residuei376 – 3761N6-acetyllysineBy similarity
    Modified residuei508 – 5081N6-acetyllysine1 Publication
    Modified residuei700 – 7001N6-acetyllysine1 Publication
    Modified residuei781 – 7811N6-acetyllysine1 Publication
    Modified residuei837 – 8371N6-acetyllysine1 Publication
    Modified residuei865 – 8651N6-acetyllysineBy similarity
    Modified residuei906 – 9061N6-acetyllysineBy similarity
    Modified residuei1071 – 10711N6-acetyllysine; alternateBy similarity
    Modified residuei1071 – 10711N6-succinyllysine; alternateBy similarity
    Modified residuei1081 – 10811Phosphoserine3 Publications
    Modified residuei1084 – 10841Phosphoserine8 Publications
    Modified residuei1089 – 10891Phosphothreonine1 Publication
    Modified residuei1338 – 13381Phosphoserine1 Publication
    Modified residuei1372 – 13721N6-acetyllysineBy similarity
    Modified residuei1459 – 14591Phosphoserine7 Publications
    Modified residuei1533 – 15331Phosphoserine2 Publications
    Modified residuei1538 – 15381N6-acetyllysineBy similarity
    Modified residuei1630 – 16301Phosphoserine1 Publication
    Modified residuei1734 – 17341Phosphoserine1 Publication
    Modified residuei2053 – 20531Phosphoserine2 Publications
    Modified residuei2152 – 21521Phosphoserine5 Publications
    Modified residuei2158 – 21581Phosphoserine1 Publication
    Modified residuei2284 – 22841Phosphoserine2 Publications
    Modified residuei2327 – 23271Phosphoserine3 Publications
    Modified residuei2336 – 23361Phosphothreonine1 Publication
    Modified residuei2414 – 24141Phosphoserine2 Publications
    Modified residuei2510 – 25101Phosphoserine1 Publication
    Modified residuei2569 – 25691N6-acetyllysine; alternateBy similarity
    Modified residuei2569 – 25691N6-succinyllysine; alternateBy similarity
    Modified residuei2575 – 25751N6-acetyllysineBy similarity
    Modified residuei2607 – 26071N6-acetyllysine1 Publication
    Modified residuei2621 – 26211N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylation extent changes in response to cell activation.11 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP21333.
    PaxDbiP21333.
    PRIDEiP21333.

    2D gel databases

    OGPiP21333.

    PTM databases

    PhosphoSiteiP21333.

    Miscellaneous databases

    PMAP-CutDBP21333.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP21333.
    BgeeiP21333.
    CleanExiHS_FLNA.
    GenevestigatoriP21333.

    Organism-specific databases

    HPAiCAB000356.
    HPA000368.
    HPA001115.
    HPA002925.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with PDLIM2 By similarity. Interacts with FCGR1A, FLNB, FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N-terminus). Interacts (via N-terminus) with TAF1B. Interacts with TMEM67 (via C-terminus) and MKS1. Interacts (via actin-binding domain) with MICALL2 (via CH domain).By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX26EBI-350432,EBI-6863741From a different organism.
    ARHGAP24Q8N2646EBI-350432,EBI-988764
    CCNB2O950678EBI-350432,EBI-375024
    CRKP461083EBI-350432,EBI-886
    FLNBO753695EBI-350432,EBI-352089
    FOXC1Q129488EBI-350432,EBI-1175253
    GRB2P629932EBI-350432,EBI-401755
    ITGB1P055565EBI-350432,EBI-703066
    ITGB1P072282EBI-350432,EBI-5606437From a different organism.
    ITGB7P260106EBI-350432,EBI-702932
    NRP1O147862EBI-350432,EBI-1187100
    OPRM1P353725EBI-350432,EBI-2624570
    PHLDB2Q86SQ02EBI-350432,EBI-2798483

    Protein-protein interaction databases

    BioGridi108605. 106 interactions.
    DIPiDIP-1136N.
    IntActiP21333. 62 interactions.
    MINTiMINT-118283.
    STRINGi9606.ENSP00000358866.

    Structurei

    Secondary structure

    1
    2647
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 434
    Helixi44 – 5714
    Helixi58 – 603
    Turni67 – 737
    Helixi75 – 8511
    Helixi100 – 11617
    Helixi126 – 1305
    Helixi134 – 14916
    Helixi168 – 17912
    Beta strandi181 – 1833
    Helixi190 – 1923
    Beta strandi193 – 1953
    Helixi196 – 20510
    Helixi213 – 2153
    Helixi221 – 23616
    Helixi244 – 2474
    Helixi254 – 2618
    Helixi263 – 2664
    Helixi480 – 4823
    Beta strandi484 – 4874
    Helixi488 – 4903
    Beta strandi501 – 5066
    Beta strandi515 – 5217
    Beta strandi529 – 5346
    Beta strandi537 – 5426
    Beta strandi548 – 5569
    Beta strandi565 – 5717
    Beta strandi579 – 5835
    Helixi584 – 5863
    Beta strandi588 – 5903
    Beta strandi595 – 60410
    Beta strandi609 – 6179
    Beta strandi620 – 6256
    Beta strandi627 – 63610
    Beta strandi639 – 64911
    Beta strandi658 – 6647
    Helixi672 – 6743
    Beta strandi676 – 6794
    Helixi680 – 6823
    Beta strandi683 – 6853
    Beta strandi693 – 6986
    Beta strandi707 – 7126
    Beta strandi714 – 7163
    Beta strandi721 – 7255
    Beta strandi727 – 7359
    Beta strandi739 – 74911
    Beta strandi758 – 7625
    Helixi1160 – 11623
    Beta strandi1164 – 11674
    Helixi1168 – 11703
    Beta strandi1172 – 11743
    Beta strandi1179 – 11846
    Beta strandi1193 – 11986
    Beta strandi1206 – 12116
    Beta strandi1213 – 122210
    Beta strandi1225 – 123511
    Beta strandi1244 – 12507
    Turni1785 – 17873
    Beta strandi1791 – 17966
    Beta strandi1804 – 18096
    Beta strandi1819 – 18224
    Beta strandi1824 – 18329
    Beta strandi1838 – 18469
    Beta strandi1855 – 18606
    Beta strandi1865 – 18673
    Beta strandi1869 – 18724
    Helixi1873 – 18753
    Beta strandi1877 – 18793
    Beta strandi1884 – 18896
    Turni1891 – 18933
    Beta strandi1895 – 190612
    Beta strandi1909 – 19146
    Beta strandi1916 – 192510
    Beta strandi1930 – 19389
    Beta strandi1947 – 19537
    Beta strandi1959 – 19679
    Beta strandi1980 – 19889
    Beta strandi1998 – 20014
    Beta strandi2007 – 20104
    Beta strandi2014 – 202512
    Beta strandi2034 – 20396
    Helixi2041 – 20433
    Helixi2047 – 20493
    Beta strandi2051 – 20544
    Helixi2055 – 20573
    Beta strandi2059 – 20613
    Beta strandi2066 – 20716
    Beta strandi2075 – 20773
    Beta strandi2080 – 20889
    Beta strandi2091 – 20966
    Beta strandi2100 – 21078
    Beta strandi2112 – 21209
    Beta strandi2129 – 21368
    Beta strandi2139 – 214810
    Beta strandi2174 – 21796
    Beta strandi2185 – 21895
    Beta strandi2208 – 22169
    Beta strandi2225 – 22317
    Helixi2238 – 22403
    Beta strandi2242 – 22454
    Helixi2246 – 22483
    Beta strandi2257 – 22626
    Helixi2264 – 22663
    Beta strandi2271 – 22799
    Beta strandi2282 – 22876
    Beta strandi2293 – 22986
    Beta strandi2303 – 23119
    Beta strandi2320 – 23267
    Turni2429 – 24313
    Beta strandi2433 – 24364
    Helixi2437 – 24393
    Beta strandi2441 – 24433
    Beta strandi2448 – 24536
    Turni2455 – 24573
    Beta strandi2462 – 24709
    Beta strandi2472 – 24798
    Beta strandi2482 – 24898
    Beta strandi2491 – 250616
    Beta strandi2511 – 25188
    Beta strandi2561 – 25644
    Helixi2565 – 25673
    Beta strandi2576 – 25816
    Beta strandi2590 – 25956
    Beta strandi2597 – 25993
    Beta strandi2602 – 26109
    Beta strandi2613 – 26197
    Beta strandi2624 – 26329
    Beta strandi2641 – 26466

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AAVNMR-A1863-1956[»]
    2BP3X-ray2.32A/B1863-1956[»]
    2BRQX-ray2.10A/B2236-2329[»]
    2J3SX-ray2.50A/B2045-2329[»]
    2JF1X-ray2.20A2236-2329[»]
    2K3TNMR-A2427-2522[»]
    2K7PNMR-A1772-1956[»]
    2K7QNMR-A1954-2141[»]
    2W0PX-ray1.90A/B2236-2329[»]
    2WFNX-ray3.20A/B1-278[»]
    3CNKX-ray1.65A/B2559-2647[»]
    3HOCX-ray2.30A/B2-269[»]
    3HOPX-ray2.30A/B2-269[»]
    3HORX-ray2.70A/B2-269[»]
    3ISWX-ray2.80A/B2236-2329[»]
    3RGHX-ray2.44A/B1158-1252[»]
    4M9PX-ray1.72A478-766[»]
    ProteinModelPortaliP21333.
    SMRiP21333. Positions 39-2647.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21333.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 274273Actin-bindingAdd
    BLAST
    Domaini43 – 149107CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini166 – 266101CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati276 – 37499Filamin 1Add
    BLAST
    Repeati376 – 47499Filamin 2Add
    BLAST
    Repeati475 – 57096Filamin 3Add
    BLAST
    Repeati571 – 66393Filamin 4Add
    BLAST
    Repeati667 – 76397Filamin 5Add
    BLAST
    Repeati764 – 866103Filamin 6Add
    BLAST
    Repeati867 – 96599Filamin 7Add
    BLAST
    Repeati966 – 106196Filamin 8Add
    BLAST
    Repeati1062 – 115493Filamin 9Add
    BLAST
    Repeati1155 – 124995Filamin 10Add
    BLAST
    Repeati1250 – 1349100Filamin 11Add
    BLAST
    Repeati1350 – 144293Filamin 12Add
    BLAST
    Repeati1443 – 153997Filamin 13Add
    BLAST
    Repeati1540 – 163697Filamin 14Add
    BLAST
    Repeati1649 – 174092Filamin 15Add
    BLAST
    Repeati1779 – 186082Filamin 16Add
    BLAST
    Repeati1861 – 195090Filamin 17Add
    BLAST
    Repeati1951 – 203989Filamin 18Add
    BLAST
    Repeati2042 – 213190Filamin 19Add
    BLAST
    Repeati2132 – 223099Filamin 20Add
    BLAST
    Repeati2233 – 232593Filamin 21Add
    BLAST
    Repeati2327 – 242094Filamin 22Add
    BLAST
    Repeati2424 – 251693Filamin 23Add
    BLAST
    Repeati2552 – 264695Filamin 24Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1490 – 1607118Interaction with furinBy similarityAdd
    BLAST
    Regioni1741 – 177838Hinge 1Add
    BLAST
    Regioni2517 – 2647131Self-association site, tailAdd
    BLAST
    Regioni2517 – 255135Hinge 2Add
    BLAST

    Domaini

    Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation.

    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.
    InParanoidiP21333.
    KOiK04437.
    OMAiVQVQDNE.
    PhylomeDBiP21333.
    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.
    IPR028559. FLN.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view]
    PANTHERiPTHR11915:SF173. PTHR11915:SF173. 1 hit.
    PfamiPF00307. CH. 2 hits.
    PF00630. Filamin. 23 hits.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    SM00557. IG_FLMN. 24 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF81296. SSF81296. 24 hits.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS50194. FILAMIN_REPEAT. 24 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P21333-1) [UniParc]FASTAAdd to Basket

    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

    MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT     50
    RWCNEHLKCV SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR 100
    QMQLENVSVA LEFLDRESIK LVSIDSKAIV DGNLKLILGL IWTLILHYSI 150
    SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL PQLPITNFSR DWQSGRALGA 200
    LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ VITPEEIVDP 250
    NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK 300
    RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV 350
    TGTHKVTVLF AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK 400
    TTYFEIFTAG AGTGEVEVVI QDPMGQKGTV EPQLEARGDS TYRCSYQPTM 450
    EGVHTVHVTF AGVPIPRSPY TVTVGQACNP SACRAVGRGL QPKGVRVKET 500
    ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF EYYPMVPGTY 550
    IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE 600
    AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN 650
    SEDIRLSPFM ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK 700
    HGGKAPLRVQ VQDNEGCPVE ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG 750
    GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA KTGLKAHEPT YFTVDCAEAG 800
    QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP RGAGSYTIMV 850
    LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK 900
    AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT 950
    YGGDPIPKSP FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG 1000
    QGKVASKIVG PSGAAVPCKV EPGLGADNSV VRFLPREEGP YEVEVTYDGV 1050
    PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG SAGSPARFTI DTKGAGTGGL 1100
    GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF ADTHIPGSPF 1150
    KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE 1200
    AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE 1250
    PAVDTSGVQC YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP 1300
    SGNLTETYVQ DRGDGMYKVE YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT 1350
    EGCDPSRVRV HGPGIQSGTT NKPNKFTVET RGAGTGGLGL AVEGPSEAKM 1400
    SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV PVHDVTDASK 1450
    VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV 1500
    DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA 1550
    SGPGLNTTGV PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH 1600
    DGTYTVAYVP DVTGRYTILI KYGGDEIPFS PYRVRAVPTG DASKCTVTVS 1650
    IGGHGLGAGI GPTIQIGEET VITVDTKAAG KGKVTCTVCT PDGSEVDVDV 1700
    VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA LAGDQPSVQP 1750
    PLRSQQLAPQ YTYAQGGQQT WAPERPLVGV NGLDVTSLRP FDLVIPFTIK 1800
    KGEITGEVRM PSGKVAQPTI TDNKDGTVTV RYAPSEAGLH EMDIRYDNMH 1850
    IPGSPLQFYV DYVNCGHVTA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL 1900
    AIEGPSKAEI SCTDNQDGTC SVSYLPVLPG DYSILVKYNE QHVPGSPFTA 1950
    RVTGDDSMRM SHLKVGSAAD IPINISETDL SLLTATVVPP SGREEPCLLK 2000
    RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS QSEIGDASRV 2050
    RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG 2100
    TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA 2150
    PSVANVGSHC DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI 2200
    RFVPAEMGTH TVSVKYKGQH VPGSPFQFTV GPLGEGGAHK VRAGGPGLER 2250
    AEAGVPAEFS IWTREAGAGG LAIAVEGPSK AEISFEDRKD GSCGVAYVVQ 2300
    EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL QESGLKVNQP 2350
    ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGVY 2400
    LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGNPAEF 2450
    VVNTSNAGAG ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK 2500
    YGGPYHIGGS PFKAKVTGPR LVSNHSLHET SSVFVDSLTK ATCAPQHGAP 2550
    GPGPADASKV VAKGLGLSKA YVGQKSSFTV DCSKAGNNML LVGVHGPRTP 2600
    CEEILVKHVG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRVVVP 2647
    Length:2,647
    Mass (Da):280,739
    Last modified:January 23, 2007 - v4
    Checksum:i6C1A07041DF50142
    GO
    Isoform 2 (identifier: P21333-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1649-1656: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,639
    Mass (Da):280,018
    Checksum:i862625C6FEA39075
    GO

    Sequence cautioni

    The sequence BAC03408.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441I → T AA sequence (PubMed:2248958)Curated
    Sequence conflicti1772 – 17721A → G in CAA49687. (PubMed:7689010)Curated
    Sequence conflicti2341 – 23411Q → R in BAC03408. (PubMed:14702039)Curated
    Sequence conflicti2634 – 26341D → H in CAA37495. (PubMed:8088819)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391A → G in PVNH4. 1 Publication
    VAR_022734
    Natural varianti82 – 821E → V in PVNH1. 1 Publication
    Corresponds to variant rs28935169 [ dbSNP | Ensembl ].
    VAR_015699
    Natural varianti102 – 1021M → V in PVNH1. 1 Publication
    VAR_031305
    Natural varianti128 – 1281A → V in PVNH4. 1 Publication
    VAR_031306
    Natural varianti149 – 1491S → F in PVNH1. 1 Publication
    VAR_031307
    Natural varianti170 – 1701Q → P in OPD2. 1 Publication
    VAR_015713
    Natural varianti172 – 1721L → F in OPD1. 1 Publication
    VAR_015714
    Natural varianti196 – 1961R → G in OPD2. 1 Publication
    VAR_015715
    Natural varianti196 – 1961R → W in OPD1. 1 Publication
    VAR_015716
    Natural varianti200 – 2001A → S in OPD2. 1 Publication
    VAR_015717
    Natural varianti203 – 2031D → Y in OPD1. 1 Publication
    VAR_031308
    Natural varianti207 – 2071P → L in OPD1. 1 Publication
    Corresponds to variant rs28935469 [ dbSNP | Ensembl ].
    VAR_015700
    Natural varianti210 – 2101C → F in OPD2. 1 Publication
    VAR_058720
    Natural varianti254 – 2541E → K in OPD2. 1 Publication
    Corresponds to variant rs28935470 [ dbSNP | Ensembl ].
    VAR_015701
    Natural varianti273 – 2731A → P in OPD2. 1 Publication
    VAR_015718
    Natural varianti288 – 2881G → R in CVDX. 1 Publication
    VAR_064156
    Natural varianti320 – 3201V → A.
    Corresponds to variant rs1064816 [ dbSNP | Ensembl ].
    VAR_012831
    Natural varianti370 – 3701F → L.
    Corresponds to variant rs1064817 [ dbSNP | Ensembl ].
    VAR_012832
    Natural varianti429 – 4291T → M.1 Publication
    VAR_069803
    Natural varianti528 – 5281V → M in PVNH1. 1 Publication
    Corresponds to variant rs143873938 [ dbSNP | Ensembl ].
    VAR_031309
    Natural varianti552 – 5521V → A.
    Corresponds to variant rs730319 [ dbSNP | Ensembl ].
    VAR_012833
    Natural varianti555 – 5551T → K in OPD2. 1 Publication
    VAR_015719
    Natural varianti637 – 6371P → Q in CVDX. 1 Publication
    VAR_064157
    Natural varianti656 – 6561L → F in PVNH1. 1 Publication
    VAR_012834
    Natural varianti711 – 7111V → D in CVDX. 1 Publication
    VAR_064158
    Natural varianti1012 – 10121S → L.
    Corresponds to variant rs17091204 [ dbSNP | Ensembl ].
    VAR_031310
    Natural varianti1159 – 11591D → A in FMD; does not inhibit interaction with MIS18BP1. 1 Publication
    Corresponds to variant rs28935471 [ dbSNP | Ensembl ].
    VAR_015702
    Natural varianti1184 – 11841D → E in MNS. 1 Publication
    VAR_015720
    Natural varianti1186 – 11861S → L in FMD. 2 Publications
    VAR_015721
    Natural varianti1188 – 11881A → T in MNS; does not inhibit interaction with MIS18BP1. 1 Publication
    Corresponds to variant rs28935472 [ dbSNP | Ensembl ].
    VAR_015703
    Natural varianti1199 – 11991S → L in MNS; does not inhibit interaction with MIS18BP1. 1 Publication
    Corresponds to variant rs28935473 [ dbSNP | Ensembl ].
    VAR_015704
    Natural varianti1291 – 12911P → L in FGS2. 1 Publication
    VAR_058721
    Natural varianti1419 – 14191A → G.
    Corresponds to variant rs35504556 [ dbSNP | Ensembl ].
    VAR_032083
    Natural varianti1620 – 16201Missing in FMD. 1 Publication
    VAR_015722
    Natural varianti1635 – 16373Missing in otopalatodigital spectrum disorder. 1 Publication
    VAR_031311
    Natural varianti1645 – 16451C → F in OPD2. 1 Publication
    VAR_015723
    Natural varianti1724 – 173916Missing in TOD. 1 Publication
    VAR_064159Add
    BLAST
    Natural varianti1728 – 17281G → C in FMD. 1 Publication
    VAR_031312
    Natural varianti1764 – 17641A → T.2 Publications
    Corresponds to variant rs57108893 [ dbSNP | Ensembl ].
    VAR_012835
    Natural varianti1803 – 18031E → K Probable disease-associated mutation found in a patient with macrothrombocytopenia. 1 Publication
    VAR_067251

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1649 – 16568Missing in isoform 2. 1 PublicationVSP_035454

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53416 mRNA. Translation: CAA37495.1.
    L44140 Genomic DNA. Translation: AAA92644.1.
    X70082 Genomic DNA. Translation: CAA49687.1.
    X70085 Genomic DNA. Translation: CAA49690.1.
    GU727643 mRNA. Translation: ADU87644.1.
    AK090427 mRNA. Translation: BAC03408.2. Different initiation.
    AB593010 mRNA. Translation: BAJ83965.1.
    BX664723, BX936346 Genomic DNA. Translation: CAI43197.1.
    BX664723, BX936346 Genomic DNA. Translation: CAI43199.1.
    BX936346, BX664723 Genomic DNA. Translation: CAI43225.1.
    BX936346, BX664723 Genomic DNA. Translation: CAI43227.1.
    CH471172 Genomic DNA. Translation: EAW72745.1.
    CH471172 Genomic DNA. Translation: EAW72746.1.
    CCDSiCCDS44021.1. [P21333-2]
    CCDS48194.1. [P21333-1]
    PIRiA37098.
    RefSeqiNP_001104026.1. NM_001110556.1. [P21333-1]
    NP_001447.2. NM_001456.3. [P21333-2]
    UniGeneiHs.195464.

    Genome annotation databases

    EnsembliENST00000360319; ENSP00000353467; ENSG00000196924. [P21333-2]
    ENST00000369850; ENSP00000358866; ENSG00000196924. [P21333-1]
    ENST00000422373; ENSP00000416926; ENSG00000196924. [P21333-2]
    GeneIDi2316.
    KEGGihsa:2316.
    UCSCiuc004fkk.2. human. [P21333-1]
    uc010nuu.1. human. [P21333-2]

    Polymorphism databases

    DMDMi116241365.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53416 mRNA. Translation: CAA37495.1 .
    L44140 Genomic DNA. Translation: AAA92644.1 .
    X70082 Genomic DNA. Translation: CAA49687.1 .
    X70085 Genomic DNA. Translation: CAA49690.1 .
    GU727643 mRNA. Translation: ADU87644.1 .
    AK090427 mRNA. Translation: BAC03408.2 . Different initiation.
    AB593010 mRNA. Translation: BAJ83965.1 .
    BX664723 , BX936346 Genomic DNA. Translation: CAI43197.1 .
    BX664723 , BX936346 Genomic DNA. Translation: CAI43199.1 .
    BX936346 , BX664723 Genomic DNA. Translation: CAI43225.1 .
    BX936346 , BX664723 Genomic DNA. Translation: CAI43227.1 .
    CH471172 Genomic DNA. Translation: EAW72745.1 .
    CH471172 Genomic DNA. Translation: EAW72746.1 .
    CCDSi CCDS44021.1. [P21333-2 ]
    CCDS48194.1. [P21333-1 ]
    PIRi A37098.
    RefSeqi NP_001104026.1. NM_001110556.1. [P21333-1 ]
    NP_001447.2. NM_001456.3. [P21333-2 ]
    UniGenei Hs.195464.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AAV NMR - A 1863-1956 [» ]
    2BP3 X-ray 2.32 A/B 1863-1956 [» ]
    2BRQ X-ray 2.10 A/B 2236-2329 [» ]
    2J3S X-ray 2.50 A/B 2045-2329 [» ]
    2JF1 X-ray 2.20 A 2236-2329 [» ]
    2K3T NMR - A 2427-2522 [» ]
    2K7P NMR - A 1772-1956 [» ]
    2K7Q NMR - A 1954-2141 [» ]
    2W0P X-ray 1.90 A/B 2236-2329 [» ]
    2WFN X-ray 3.20 A/B 1-278 [» ]
    3CNK X-ray 1.65 A/B 2559-2647 [» ]
    3HOC X-ray 2.30 A/B 2-269 [» ]
    3HOP X-ray 2.30 A/B 2-269 [» ]
    3HOR X-ray 2.70 A/B 2-269 [» ]
    3ISW X-ray 2.80 A/B 2236-2329 [» ]
    3RGH X-ray 2.44 A/B 1158-1252 [» ]
    4M9P X-ray 1.72 A 478-766 [» ]
    ProteinModelPortali P21333.
    SMRi P21333. Positions 39-2647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108605. 106 interactions.
    DIPi DIP-1136N.
    IntActi P21333. 62 interactions.
    MINTi MINT-118283.
    STRINGi 9606.ENSP00000358866.

    PTM databases

    PhosphoSitei P21333.

    Polymorphism databases

    DMDMi 116241365.

    2D gel databases

    OGPi P21333.

    Proteomic databases

    MaxQBi P21333.
    PaxDbi P21333.
    PRIDEi P21333.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360319 ; ENSP00000353467 ; ENSG00000196924 . [P21333-2 ]
    ENST00000369850 ; ENSP00000358866 ; ENSG00000196924 . [P21333-1 ]
    ENST00000422373 ; ENSP00000416926 ; ENSG00000196924 . [P21333-2 ]
    GeneIDi 2316.
    KEGGi hsa:2316.
    UCSCi uc004fkk.2. human. [P21333-1 ]
    uc010nuu.1. human. [P21333-2 ]

    Organism-specific databases

    CTDi 2316.
    GeneCardsi GC0XM153576.
    GeneReviewsi FLNA.
    H-InvDB HIX0017150.
    HGNCi HGNC:3754. FLNA.
    HPAi CAB000356.
    HPA000368.
    HPA001115.
    HPA002925.
    MIMi 300017. gene.
    300048. phenotype.
    300049. phenotype.
    300244. phenotype.
    300321. phenotype.
    300537. phenotype.
    304120. phenotype.
    305620. phenotype.
    309350. phenotype.
    311300. phenotype.
    314400. phenotype.
    neXtProti NX_P21333.
    Orphaneti 2978. Chronic intestinal pseudoobstruction.
    2301. Congenital short bowel syndrome.
    1864. Congenital valvular dysplasia.
    82004. Ehlers-Danlos syndrome with periventricular heterotopia.
    323. FG syndrome.
    1826. Frontometaphyseal dysplasia.
    2484. Osteodysplasty, Melnick-Needles type.
    90650. Otopalatodigital syndrome type 1.
    90652. Otopalatodigital syndrome type 2.
    98892. Periventricular nodular heterotopia.
    88630. Terminal osseous dysplasia - pigmentary defects.
    PharmGKBi PA28172.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000044235.
    HOVERGENi HBG004163.
    InParanoidi P21333.
    KOi K04437.
    OMAi VQVQDNE.
    PhylomeDBi P21333.
    TreeFami TF313685.

    Enzyme and pathway databases

    Reactomei REACT_20649. Cell-extracellular matrix interactions.
    REACT_23847. GP1b-IX-V activation signalling.
    SignaLinki P21333.

    Miscellaneous databases

    ChiTaRSi FLNA. human.
    EvolutionaryTracei P21333.
    GeneWikii FLNA.
    GenomeRNAii 2316.
    NextBioi 9405.
    PMAP-CutDB P21333.
    PROi P21333.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21333.
    Bgeei P21333.
    CleanExi HS_FLNA.
    Genevestigatori P21333.

    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.
    IPR028559. FLN.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view ]
    PANTHERi PTHR11915:SF173. PTHR11915:SF173. 1 hit.
    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 endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring."
      Gorlin J.B., Yamin R., Egan S., Stewart M., Stossel T.P., Kwiatkowski D.J., Hartwig J.H.
      J. Cell Biol. 111:1089-1105(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "The exon-intron organization of the human X-linked gene (FLN1) encoding actin-binding protein 280."
      Patrosso M.C., Repetto M., Villa A., Milanesi L., Frattini A., Faranda S., Mancini M., Maestrini E., Toniolo D., Vezzoni P.
      Genomics 21:71-76(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
      Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
      Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
      Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
      Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Spleen.
    6. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
      Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
      Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Tissue: Platelet.
    10. "Purification of human smooth muscle filamin and characterization of structural domains and functional sites."
      Hock R.S., Davis G., Speicher D.W.
      Biochemistry 29:9441-9451(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-54; 917-940; 1037-1050; 1754-1783 AND 2148-2168.
    11. "Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7."
      Maestrini E., Patrosso C., Mancini M., Rivella S., Rocchi M., Repetto M., Villa A., Frattini A., Zoppe M., Vezzoni P., Toniolo D.
      Hum. Mol. Genet. 2:761-766(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1658-1772.
    12. "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: SIMILARITY TO OTHER MEMBERS OF THE FAMILY.
    13. "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: INTERACTION WITH PSEN1 AND PSEN2.
    14. "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin."
      Petrecca K., Miller D.M., Shrier A.
      J. Neurosci. 20:8736-8744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCND2.
    15. "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: INTERACTION WITH INPPL1.
    16. "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 FLNB.
    17. "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 MYOT AND MYOZ1.
    18. Cited for: REVIEW.
    19. Cited for: REVIEW.
    20. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089; SER-1459; SER-2152 AND SER-2284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "A filamin A splice mutation resulting in a syndrome of facial dysmorphism, periventricular nodular heterotopia, and severe constipation reminiscent of cerebro-fronto-facial syndrome."
      Hehr U., Hehr A., Uyanik G., Phelan E., Winkler J., Reardon W.
      J. Med. Genet. 43:541-544(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PVNH1.
    22. "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-1084 AND SER-1459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling."
      Ohta Y., Hartwig J.H., Stossel T.P.
      Nat. Cell Biol. 8:803-814(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP24.
    24. "Filamin A is mutated in X-linked chronic idiopathic intestinal pseudo-obstruction with central nervous system involvement."
      Gargiulo A., Auricchio R., Barone M.V., Cotugno G., Reardon W., Milla P.J., Ballabio A., Ciccodicola A., Auricchio A.
      Am. J. Hum. Genet. 80:751-758(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN IPOX.
    25. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: INTERACTION WITH ECSCR.
    27. Cited for: INTERACTION WITH FCGR1A.
    28. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459; SER-2152 AND SER-2158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    31. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1338; SER-1459; SER-1533; SER-1630; SER-2053; SER-2152; SER-2327; SER-2414 AND SER-2510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "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-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    35. "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-508; LYS-700; LYS-781; LYS-837; LYS-2607 AND LYS-2621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "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 SER-1081; SER-1084; SER-1459; SER-1533; SER-1734; SER-2053; SER-2152; SER-2284; SER-2327; THR-2336 AND SER-2414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "Identification of novel nuclear protein interactions with the N-terminal part of filamin A."
      Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K.
      Biosci. Biotechnol. Biochem. 75:145-147(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAF1B AND MIS18BP1, CHARACTERIZATION OF VARIANTS ALA-1159; THR-1188 AND LEU-1199.
    39. Cited for: INVOLVEMENT IN MACROTHROMBOCYTOPENIA, VARIANT LYS-1803.
    40. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-1081; SER-1084; SER-1459; SER-2152 AND SER-2327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. Cited for: FUNCTION IN CILIOGENESIS, INTERACTION WITH TMEM67 AND MKS1.
    42. "Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins."
      Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., Imoto I., Matsushita N., Sasaki T.
      Genes Cells 18:810-822(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICALL2.
    43. "Congenital short bowel syndrome as the presenting symptom in male patients with FLNA mutations."
      van der Werf C.S., Sribudiani Y., Verheij J.B., Carroll M., O'Loughlin E., Chen C.H., Brooks A.S., Liszewski M.K., Atkinson J.P., Hofstra R.M.
      Genet. Med. 15:310-313(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CSBSX.
    44. "Structure of three tandem filamin domains reveals auto-inhibition of ligand binding."
      Lad Y., Kiema T., Jiang P., Pentikainen O.T., Coles C.H., Campbell I.D., Calderwood D.A., Ylanne J.
      EMBO J. 26:3993-4004(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2045-2329.
    45. "Structure of the human filamin A actin-binding domain."
      Ruskamo S., Ylanne J.
      Acta Crystallogr. D 65:1217-1221(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-278, ACTIN-BINDING REGION, SUBUNIT.
    46. "Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin."
      Heikkinen O.K., Ruskamo S., Konarev P.V., Svergun D.I., Iivanainen T., Heikkinen S.M., Permi P., Koskela H., Kilpelainen I., Ylanne J.
      J. Biol. Chem. 284:25450-25458(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1772-1956 AND 1954-2141.
    47. Cited for: VARIANT PVNH1 PHE-656, VARIANT THR-1764.
    48. "Bilateral periventricular nodular heterotopia due to filamin 1 gene mutation: widespread glomeruloid microvascular anomaly and dysplastic cytoarchitecture in the cerebral cortex."
      Kakita A., Hayashi S., Moro F., Guerrini R., Ozawa T., Ono K., Kameyama S., Walsh C.A., Takahashi H.
      Acta Neuropathol. 104:649-657(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PVNH1 MET-528.
    49. "Familial periventricular heterotopia: missense and distal truncating mutations of the FLN1 gene."
      Moro F., Carrozzo R., Veggiotti P., Tortorella G., Toniolo D., Volzone A., Guerrini R.
      Neurology 58:916-921(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PVNH1 VAL-82.
    50. Cited for: VARIANTS OPD1 PHE-172; TRP-196 AND LEU-207, VARIANTS OPD2 PRO-170; GLY-196; SER-200; LYS-254; PRO-273; LYS-555 AND PHE-1645, VARIANTS FMD ALA-1159; LEU-1186 AND ILE-1620 DEL, VARIANTS MNS GLU-1184; THR-1188 AND LEU-1199, VARIANTS MET-429 AND THR-1764.
    51. "Germline and mosaic mutations of FLN1 in men with periventricular heterotopia."
      Guerrini R., Mei D., Sisodiya S.M., Sicca F., Harding B., Takahashi Y., Dorn T., Yoshida A., Campistol J., Kraemer G., Moro F., Dobyns W.B.,