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P21333

- FLNA_HUMAN

UniProt

P21333 - FLNA_HUMAN

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Protein
Filamin-A
Gene
FLNA, FLN, FLN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Sites

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

GO - Molecular functioni

  1. Fc-gamma receptor I complex binding Source: BHF-UCL
  2. Rac GTPase binding Source: BHF-UCL
  3. Ral GTPase binding Source: BHF-UCL
  4. Rho GTPase binding Source: BHF-UCL
  5. actin filament binding Source: BHF-UCL
  6. glycoprotein binding Source: BHF-UCL
  7. poly(A) RNA binding Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. protein homodimerization activity 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
Complete GO annotation...

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1159 – 11591D → A in FMD; does not inhibit interaction with MIS18BP1. 2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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. 2 Publications
Corresponds to variant rs28935472 [ dbSNP | Ensembl ].
VAR_015703
Natural varianti1199 – 11991S → L in MNS; does not inhibit interaction with MIS18BP1. 2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1724 – 173916Missing in TOD.
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 11Removed1 Publication
Chaini2 – 26472646Filamin-A
PRO_0000087296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei376 – 3761N6-acetyllysine By similarity
Modified residuei508 – 5081N6-acetyllysine1 Publication
Modified residuei700 – 7001N6-acetyllysine1 Publication
Modified residuei781 – 7811N6-acetyllysine1 Publication
Modified residuei837 – 8371N6-acetyllysine1 Publication
Modified residuei865 – 8651N6-acetyllysine By similarity
Modified residuei906 – 9061N6-acetyllysine By similarity
Modified residuei1071 – 10711N6-acetyllysine; alternate By similarity
Modified residuei1071 – 10711N6-succinyllysine; alternate By similarity
Modified residuei1081 – 10811Phosphoserine3 Publications
Modified residuei1084 – 10841Phosphoserine8 Publications
Modified residuei1089 – 10891Phosphothreonine1 Publication
Modified residuei1338 – 13381Phosphoserine1 Publication
Modified residuei1372 – 13721N6-acetyllysine By similarity
Modified residuei1459 – 14591Phosphoserine7 Publications
Modified residuei1533 – 15331Phosphoserine2 Publications
Modified residuei1538 – 15381N6-acetyllysine By 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; alternate By similarity
Modified residuei2569 – 25691N6-succinyllysine; alternate By similarity
Modified residuei2575 – 25751N6-acetyllysine By similarity
Modified residuei2607 – 26071N6-acetyllysine1 Publication
Modified residuei2621 – 26211N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylation extent changes in response to cell activation.

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).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX26EBI-350432,EBI-6863748From a different organism.
ARHGAP24Q8N2646EBI-350432,EBI-988764
CCNB2O950678EBI-350432,EBI-375024
CRKP461082EBI-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. 55 interactions.
MINTiMINT-118283.
STRINGi9606.ENSP00000358866.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP21333.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1490 – 1607118Interaction with furin By similarity
Add
BLAST
Regioni1741 – 177838Hinge 1
Add
BLAST
Regioni2517 – 2647131Self-association site, tail
Add
BLAST
Regioni2517 – 255135Hinge 2
Add
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.
Contains 24 filamin repeats.

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.

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. 2 Publications
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. 2 Publications
Corresponds to variant rs28935472 [ dbSNP | Ensembl ].
VAR_015703
Natural varianti1199 – 11991S → L in MNS; does not inhibit interaction with MIS18BP1. 2 Publications
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.
VAR_031311
Natural varianti1645 – 16451C → F in OPD2. 1 Publication
VAR_015723
Natural varianti1724 – 173916Missing in TOD.
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.
VSP_035454

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441I → T AA sequence 1 Publication
Sequence conflicti1772 – 17721A → G in CAA49687. 1 Publication
Sequence conflicti2341 – 23411Q → R in BAC03408. 1 Publication
Sequence conflicti2634 – 26341D → H in CAA37495. 1 Publication

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]
ENST00000596447; ENSP00000469433; ENSG00000269329. [P21333-2]
ENST00000597475; ENSP00000471999; ENSG00000269329. [P21333-2]
ENST00000600520; ENSP00000472325; ENSG00000269329. [P21333-1]
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. 55 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 ]
ENST00000596447 ; ENSP00000469433 ; ENSG00000269329 . [P21333-2 ]
ENST00000597475 ; ENSP00000471999 ; ENSG00000269329 . [P21333-2 ]
ENST00000600520 ; ENSP00000472325 ; ENSG00000269329 . [P21333-1 ]
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

« Hide 'large scale' publications
  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. Cited for: VARIANTS PVNH1 VAL-102 AND PHE-149.
  52. "A novel 9 bp deletion in the filamin A gene causes an otopalatodigital-spectrum disorder with a variable, intermediate phenotype."
    Stefanova M., Meinecke P., Gal A., Bolz H.
    Am. J. Med. Genet. A 132:386-390(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OTOPALATODIGITAL SPECTRUM DISORDER 1635-ARG--VAL-1637 DEL.
  53. "A novel filamin A D203Y mutation in a female patient with otopalatodigital type 1 syndrome and extremely skewed X chromosome inactivation."
    Hidalgo-Bravo A., Pompa-Mera E.N., Kofman-Alfaro S., Gonzalez-Bonilla C.R., Zenteno J.C.
    Am. J. Med. Genet. A 136:190-193(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPD1 TYR-203.
  54. Cited for: VARIANT PVNH4 GLY-39.
  55. "Genotype-epigenotype-phenotype correlations in females with frontometaphyseal dysplasia."
    Zenker M., Naehrlich L., Sticht H., Reis A., Horn D.
    Am. J. Med. Genet. A 140:1069-1073(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FMD LEU-1186 AND CYS-1728.
  56. "Ehlers-Danlos syndrome and periventricular nodular heterotopia in a Spanish family with a single FLNA mutation."
    Gomez-Garre P., Seijo M., Gutierrez-Delicado E., Castro del Rio M., de la Torre C., Gomez-Abad C., Morales-Corraliza J., Puig M., Serratosa J.M.
    J. Med. Genet. 43:232-237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PVNH4 VAL-128.
  57. "Otopalatodigital syndrome type 2 in two siblings with a novel filamin A 629G>T mutation: clinical, pathological, and molecular findings."
    Marino-Enriquez A., Lapunzina P., Robertson S.P., Rodriguez J.I.
    Am. J. Med. Genet. A 143:1120-1125(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPD2 PHE-210.
  58. Cited for: VARIANT FGS2 LEU-1291.
  59. Cited for: VARIANTS CVDX ARG-288; GLN-637 AND ASP-711.
  60. Cited for: VARIANT TOD 1724-VAL--THR-1739 DEL.

Entry informationi

Entry nameiFLNA_HUMAN
AccessioniPrimary (citable) accession number: P21333
Secondary accession number(s): E9KL45
, Q5HY53, Q5HY55, Q8NF52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 189 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

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    Human chromosome X: 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

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