FLNA
entrez
2316
canonical
uniprot
P21333
canonical
ensembl
ENSG00000196924
resolver
ensp
ENSP00000353467
resolver
ensp
ENSP00000358866
resolver
ensp
ENSP00000358872
resolver
enst
ENST00000369856
resolver
genesymbol
FLNA
resolver
genesymbol_syn
FLN
resolver
genesymbol_syn
FLN1
resolver
hgnc
HGNC:3754
resolver
uniprot
A0ACM8Q5Q1
resolver
uniprot
E9KL45
resolver
uniprot
E9PHF0
resolver
uniprot
Q5HY53
resolver
uniprot
Q5HY55
resolver
uniprot
Q60FE5
resolver
uniprot
Q6NXF2
resolver
uniprot
Q8NF52
resolver
uniprot_entry
A0ACM8Q5Q1_HUMAN
resolver
uniprot_entry
FLNA_HUMAN
resolver
uniprot_entry
Q60FE5_HUMAN
resolver
uniprot_entry
Q6NXF2_HUMAN
resolver
uniprot_sec
E9KL45
resolver
uniprot_sec
E9PHF0
resolver
uniprot_sec
Q5HY53
resolver
uniprot_sec
Q5HY55
resolver
uniprot_sec
Q8NF52
resolver
amino_acid_sequence
MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP
uniprot
proteins
disease_involvement
DISEASE: 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. {ECO:0000269|PubMed:11532987, ECO:0000269|PubMed:11914408, ECO:0000269|PubMed:15249610, ECO:0000269|PubMed:15668422, ECO:0000269|PubMed:15994863, ECO:0000269|PubMed:16299064}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Otopalatodigital syndrome 1 (OPD1) [MIM:311300]: X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild intellectual disability, 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. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:15940695, ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: 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. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:17431908, ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Frontometaphyseal dysplasia 1 (FMD1) [MIM:305620]: An X-linked disease characterized by generalized skeletal dysplasia, deafness, and urogenital defects. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:16596676, ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: 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. {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-linked (CIIPX) [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. {ECO:0000269|PubMed:17357080}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X-linked disorder characterized by intellectual disability, relative macrocephaly, hypotonia and constipation. {ECO:0000269|PubMed:17632775}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: 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. {ECO:0000269|PubMed:20598277}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiac valvular dysplasia, X-linked (CVDPX) [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. {ECO:0000269|PubMed:17190868}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abnormally enlarged (PubMed:21960593). {ECO:0000269|PubMed:21960593}.; DISEASE: 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. {ECO:0000269|PubMed:23037936}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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 FLNB 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. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:22121117, ECO:0000269|PubMed:25358863}.
uniprot
proteins
mass_dalton
280739
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="K->R: Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-43 and R-135."; /evidence="ECO:0000269|PubMed:24052262"; MUTAGEN 43; /note="K->R: Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-42 and R-135."; /evidence="ECO:0000269|PubMed:24052262"; MUTAGEN 135; /note="K->R: Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-42 and R-43."; /evidence="ECO:0000269|PubMed:24052262
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA. {ECO:0000269|PubMed:25666618}.; PTM: Phosphorylation extent changes in response to cell activation.; PTM: Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines (PubMed:24052262). Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome (PubMed:26766444). {ECO:0000269|PubMed:24052262, ECO:0000269|PubMed:26766444}.
uniprot
proteins
protein_family
Filamin family
uniprot
proteins
pubmed
11102480
uniprot
proteins
pubmed
11153914
uniprot
proteins
pubmed
11252955
uniprot
proteins
pubmed
11336782
uniprot
proteins
pubmed
11532987
uniprot
proteins
pubmed
11739414
uniprot
proteins
pubmed
11807098
uniprot
proteins
pubmed
11914408
uniprot
proteins
pubmed
12393796
uniprot
proteins
pubmed
12410386
uniprot
proteins
pubmed
12612583
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15249610
uniprot
proteins
pubmed
15654694
uniprot
proteins
pubmed
15668422
uniprot
proteins
pubmed
15684392
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15940695
uniprot
proteins
pubmed
15994863
uniprot
proteins
pubmed
16076904
uniprot
proteins
pubmed
16291724
uniprot
proteins
pubmed
16299064
uniprot
proteins
pubmed
16596676
uniprot
proteins
pubmed
16862148
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17190868
uniprot
proteins
pubmed
17357080
uniprot
proteins
pubmed
17431908
uniprot
proteins
pubmed
17632775
uniprot
proteins
pubmed
17690686
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18322202
uniprot
proteins
pubmed
18556573
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19622754
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19828450
uniprot
proteins
pubmed
19923718
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20598277
uniprot
proteins
pubmed
20713593
uniprot
proteins
pubmed
20736409
uniprot
proteins
pubmed
20844545
uniprot
proteins
pubmed
21228480
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21524097
uniprot
proteins
pubmed
21697133
uniprot
proteins
pubmed
21960593
uniprot
proteins
pubmed
22121117
uniprot
proteins
pubmed
2248958
uniprot
proteins
pubmed
23037936
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23890175
uniprot
proteins
pubmed
2391361
uniprot
proteins
pubmed
24052262
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25358863
uniprot
proteins
pubmed
25666618
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26460884
uniprot
proteins
pubmed
26766444
uniprot
proteins
pubmed
27193221
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30500825
uniprot
proteins
pubmed
30990684
uniprot
proteins
pubmed
7689010
uniprot
proteins
pubmed
8088819
uniprot
proteins
pubmed
8733135
uniprot
proteins
pubmed
9437013
uniprot
proteins
sequence_length
2647
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:16291724}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8BTM8}. Perikaryon {ECO:0000250|UniProtKB:Q8BTM8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8BTM8}. Cell projection, podosome {ECO:0000250|UniProtKB:Q8BTM8}. Note=Colocalizes with CPMR1 in the central region of DRG neuron growth cone (By similarity). Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By similarity). Localized to the core of myotube podosomes (By similarity). {ECO:0000250|UniProtKB:Q8BTM8}.
uniprot
proteins