1: FLNA filamin A, alpha [ Homo sapiens ]

GeneID: 2316 updated 25-Nov-2009

[Top][Help]Summary

Official Symbol
FLNAprovided by HGNC
Official Full Name
filamin A, alphaprovided by HGNC
Primary Source
HGNC:3754
Locus Tag
XX-FW83128A1.1
See related
Ensembl:ENSG00000196924; HPRD:02060; MIM:300017
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
FLN; FMD; MNS; OPD; ABPX; FLN1; NHBP; OPD1; OPD2; ABP-280; DKFZp434P031; FLNA
Summary
The protein encoded by this gene is an actin-binding protein that crosslinks actin filaments and links actin filaments to membrane glycoproteins. The encoded protein is involved in remodeling the cytoskeleton to effect changes in cell shape and migration. This protein interacts with integrins, transmembrane receptor complexes, and second messengers. Defects in this gene are a cause of several syndromes, including periventricular nodular heterotopias (PVNH1, PVNH4), otopalatodigital syndromes (OPD1, OPD2), frontometaphyseal dysplasia (FMD), Melnick-Needles syndrome (MNS), and X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX). Two transcript variants encoding different isoforms have been found for this gene.

[Top][Help]Genomic regions, transcripts, and products

(minus strand) Go to reference sequence detailsTry our new Sequence Viewer


[Top][Help]Genomic context

chromosome: X; Location: Xq28See FLNA in MapViewer

[Top][Help]Bibliography

Related Articles in PubMed

GeneRIFs: Gene References Into Function What's a GeneRIF?

PubMed 1. Mechanical force applied to filamin can expose cryptic integrin binding sites.
PubMed 2. These findings support a role for FLNa-beta1 integrin as a mechanosensitive complex that bidirectionally senses the tension of the matrix and, in turn, regulates cellular contractility and response to this matrix tension.
PubMed 3. propose that binding of pro-PrP to FLNa perturbs FLNa function, thus contributing to the aggressiveness of pancreatic ductal adenocarcinoma
PubMed 4. High plasma filamin A is associated with high-grade astrocytoma and metastatic breast cancer.
PubMed 5. Wnt5A activates calpain-1, leading to the cleavage of filamin A, which results in a remodeling of the cytoskeleton and an increase in melanoma cell motility
PubMed 6. The interaction between FilGAP and FlnA plays a role in protecting cells against force-induced apoptosis.
PubMed 7. Mutational analysis informed by structure can generate reagents for probing specific cellular interactions of filamin A (FLNa). Disease-related FLNa mutations have demonstrable effects on FLNa function
PubMed 8. Filamin A modulates kinase activation and intracellular trafficking of epidermal growth factor receptors in human melanoma cells.
PubMed 9. This study reports the structure of FLNa domain 24 (FLNa24), compare the structure with FLNc24, and discuss how dimerization is formed in FLNa24.
PubMed 10. FLNA genes in cell cycle control and lipid metabolism with dynamically regulated binding sites for sterol regulatory element-binding protein 1 and RNA polymerase II in HepG2 cells
PubMed 11. Our report also helps define the critical region with exclusion of FLNA in the X-linked mental retardation phenotype.
PubMed 12. analysis of the migfilin-filamin interaction and competition with integrin beta 7 tails
PubMed 13. ASB2 may regulate hematopoietic cell differentiation by modulating cell spreading and actin remodeling through targeting of filamins A and B for degradation.
PubMed 14. role of filamin cleavage and protein tyrosine phosphorylation in shear-stress-induced platelet microparticle formation and of its suppression by the monoclonal antibody (mAb) Ib-23 directed against GPIbalpha
PubMed 15. mutant FLA lacking the actin binding domain is capable of restoring almost as well as full length FLA the down-regulation of the human mu opioid receptor. Some functions of FLA do not act via the actin cytoskeleton.
PubMed 16. These data indicate that caveolin-1 specifies filamin A as a novel target for Akt-mediated filamin A Ser-2152 phosphorylation thus mediating the effects of caveolin-1 on IGF-I-induced cancer cell migration.
PubMed 17. Datas suggest that filamin A links sphingosine kinase 1 and sphingosine-1-phosphate receptor 1 to locally influence the dynamics of actin cytoskeletal structures at lamellipodia to promote cell movement.
PubMed 18. Characterize a novel cell surface protein ECSM2 that regulates endothelial chemotaxis and tube formation, and interacts with filamin A.
PubMed 19. novel mutation, c.987G-->C mutation in exon 6 of the Filamin A (FLNA) gene in the genomic DNA in bilateral periventricular nodular heterotopia
PubMed 20. Filamin A plays a pivotal role in FcgammaRI surface expression via retention of FcgammaRI from a default lysosomal pathway.
PubMed 21. Review explores the pathogenesis of persistent periventricular nodular heterotopia with respect to filamin-A (FLNa) mutations with mouse models. [review]
PubMed 22. in the absence of filamin A, chronic treatment with morphine, methadone or levorphanol leads to up-regulation of mu opioid receptor
PubMed 23. A library of FLNa fragments was generated to examine their F-actin binding to define the structural properties of FLNa that enable its various functions.
PubMed 24. analysis of filamin a IgFLN domains suggests that auto-inhibition by adjacent IgFLN domains may be a general mechanism controlling filamin-ligand interactions.
PubMed 25. FlnA restored Casodex anticaner sensitivity in C4-2 prostatic cancer cells by decreasing Akt phosphorylation.
PubMed 26. Essential for both the efficient signaling and sequestration of dopamine D3 receptor.
PubMed 27. Filamin-A as an adaptor protein that links HIV-1 receptors to the actin cytoskeleton remodelling machinery, which may facilitate virus infection.
PubMed 28. calmodulin and calcium regulate the binding of filamin A to actin filaments
PubMed 29. 3 filamin A mutations were identified in periventricular heterotopia/Ehlers-Danlos patients: a 2762 delG, a C116 point mutation causing A39G, & a 4147 delG.
PubMed 30. Periventricular nodular heterotopia caused by FLN1 mutations in men has a wide clinical spectrum and is caused by different genetic mechanisms, including somatic mosaicism.
PubMed 31. PH domain of ROCK binds to the carboxy-terminal region of filamin-A containing the last 24th repeat. ROCK co-localized with filamin-A at the protrusive cell membranes of HeLa cells.
PubMed 32. filamin-A was found to have no effect on Kir2.1 channel behavior but, rather, increased the number of functional channels resident within the membrane
PubMed 33. filamin A has a role in signaling pathways that mediate organogenesis in multiple systems during embryonic development
PubMed 34. expression of FLNa regulates constitutive activation of the Ras/ERK pathway partly through a Ras-GRF1 mechanism to modulate the production of MMP-9.
PubMed 35. FLNa may be essential for Pak1-induced cytoskeletal reorganization
PubMed 36. D3R, filamin A, and beta-arrestin form a signaling complex that is destabilized by agonist- or expression-mediated increases in GRK2/3 activity
PubMed 37. G12, Rho, filamin-A, and the actin cytoskeleton are required for amino acid-stimulated Ca2+ oscillations produced by the Ca2+-sensing receptor
PubMed 38. Data provide substantial evidence that ribosomal S6 kinase (RSK) phosphorylates filamin A, and suggest a novel role for RSK in the regulation of the actin cytoskeleton.
PubMed 39. Data indicate that filamin A binding to CD28 is required to induce the T-cell cytoskeletal rearrangements leading to recruitment of lipid microdomains and signalling mediators into the immunological synapse.
PubMed 40. shear-dependent VWF-induced platelet activation affects filamin A binding to GpIb-IX-V, and filamin A binding to the cytoplasmic tail of GpIbalpha regulates proaggregatory tyrosine kinase signaling.
PubMed 41. A purified C-terminal region of filamin is a suitable substrate for calcineurin in vitro and in vivo
PubMed 42. beta-arrestins and FLNA cooperate to regulate ERK activation and actin cytoskeleton reorganization.
PubMed 43. Filamin A is mutated in X-linked chronic idiopathic intestinal pseudo-obstruction with central nervous system involvement.
PubMed 44. Two new pedigrees of bilateral periventricular nodular heterotopia are reported with a mutation of FLN1 and a deletion in its C-terminus causing a distal protein truncation.
PubMed 45. A woman with complex partial seizures and periventricular nodular heterotopia (PNH) had an amino acid exchange, a transition of guanine to adenine at the first position of intron 13 (IVS13 + 1 G -> A) causing a splice site mutation (2022 + 1 G -> A)
PubMed 46. Dual phenotype of periventricular nodular heterotopia and frontometaphyseal dysplasia in one patient is caused by two functionally different, aberrant filamin A proteins
PubMed 47. an important role for filamin in the endocytic sorting and recycling of the internalized CTR
PubMed 48. Cell death and mechanoprotection by filamin a in connective tissues after challenge by applied tensile forces
PubMed 49. Interaction of filamin A with the insulin receptor alters insulin-dependent activation of the mitogen-activated protein kinase pathway.
PubMed 50. familial Ehlers-Danlos syndrome and periventricular nodular heterotopia is associated with an amino acid substition sssisns FLNA.
PubMed 51. there is a mechanically coupled transcriptional circuit from p38 that induces filamin-A expression [filamin A]
PubMed 52. FLNA has diverse roles in embryonic, fetal and postnatal development [review]
PubMed 53. Filamin-A interacts with c-mip/Tc-mip in a new T-cell signaling pathway.
PubMed 54. Mutations in FLNA result in frontometaphyseal dysplasia and phenotypic diversity.
PubMed 55. filamin A is the first gene known to cause isolated nonsyndromic valvular heart disease.
PubMed 56. In cells, filamin A tethered plasma membrane CFTR to the underlying actin network. This interaction stabilized CFTR at the cell surface and regulated the plasma membrane dynamics and confinement of the channel.
PubMed 57. Our results suggest a role for cyclin B1/Cdk1 in FLNa-dependent actin remodelling.
PubMed 58. FLNa interfered with androgen receptor (AR) interdomain interactions and competed with the coactivator transcriptional intermediary factor 2 to specifically down-regulate AR function.
PubMed 59. Filamin A binding to PSMA reduces the internalization rate of PSMA and its N-acelylated-alpha linked-acidic dipeptidase activity.
PubMed 60. Filamin A was identified as a direct binding partner of protein kinase Calpha; two binding sites were identified on filamin A; a Ca2+ and phospholipid-dependent association of the regulatory domain of protein kinase C with these sites was revealed.
PubMed 61. Interaction with filamin A increases cellular CaR by preventing CaR degradation, thereby facilitating CaR signaling.
PubMed 62. filamin-A has a role in the recovery from G2 arrest and subsequent mitotic cell death after DNA damage
PubMed 63. FLN1 mutations may have a role in periventricular heterotopia
PubMed 64. A novel role is revealed for filamin A in the T cell receptor/CD28 signaling pathway leading to transcription factor activation and interleukin-2 production via the inducible interaction with protein kinase C theta.
PubMed 65. This suggests that the titin Z2-Zis1 domain can link filamins and alpha-actinin together in the periphery of the Z-line/dense bodies in a fashion that is conserved in smooth and striated muscles.
PubMed 66. A novel mutation, 629G>T, in FLNA that had arisen de novo in the mother lead to Otopalatodigital syndrome type 2.

[Top][Help]HIV-1 protein interactions

Protein    Interaction
1. retropepsin A number of focal adhesion plaque proteins are specifically cleaved by HIV-1 protease, including fimbrin, focal adhesion plaque kinase (FAK), talin, and, to a lesser extent, filamin, spectrin and fibronectin PubMed

Go to the HIV-1, Human Protein Interaction Database

[Top][Help]Interactions

Description ..........
  Product Interactant Other Gene Complex Source Pubs          
 
  Filamin A   NP_061485.1   RAC1      HPRD    PubMed
 
  Filamin A   NP_149121.2   SIGLEC10      HPRD    PubMed
 
  NP_001447.1   NP_000035.2   AR      HPRD    PubMed
 
  NP_001447.1   NP_009225.1   BRCA1      HPRD    PubMed
 
  NP_001447.1   NP_000050.1   BRCA2      HPRD    PubMed
BRCA2 interacts with hsFLNa.
  NP_001447.1   NP_000050.1   BRCA2      BIND    PubMed
 
  NP_001447.1   Calcium sensing receptor   CASR      HPRD    PubMed
 
  NP_001447.1   Caveolin 1   CAV1      HPRD    PubMed
 
  NP_001447.1   NP_001782.1   CDC42      HPRD    PubMed
 
  NP_001447.1   NP_938204.1   CMIP      HPRD    PubMed
 
  NP_001447.1   NP_001911.1   DCN      HPRD    PubMed
 
  NP_001447.1   NP_000786.1   DRD2      HPRD    PubMed
Dopamine receptor D2 interacts with filamin A. This interaction was modeled on a demonstrated interaction between human FLN-A and D2 from unspecified source.
  NP_001447.1   NP_000786.1   DRD2      BIND    PubMed
Dopamine receptor D2 interacts with filamin A. This interaction was modeled on a demonstrated interaction between human FLN-A and D2 from unspecified source.
  NP_001447.1   NP_057658.2   DRD2      BIND    PubMed
 
  NP_001447.1   NP_000787.1   DRD3      HPRD    PubMed
Dopamine receptor D3 interacts with filamin A. This interaction was modeled on a demonstrated interaction between human FLN-A and D3 from unspecified source.
  NP_001447.1   NP_000787.1   DRD3      BIND    PubMed
Dopamine receptor D3 interacts with filamin A. This interaction was modeled on a demonstrated interaction between human FLN-A and D3 from unspecified source.
  NP_001447.1   NP_387512.1   DRD3      BIND    PubMed
 
  NP_001447.1   Coagulation Factor 3   F3      HPRD    PubMed
 
  NP_001447.1   NP_060026.1   FBLIM1      HPRD    PubMed
 
  NP_001447.1   Filamin B   FLNB      HPRD    PubMed
 
  NP_001447.1   Furin   FURIN      HPRD    PubMed
 
  NP_001447.1   Glycoprotein Ib, platelet, alpha polypeptide   GP1BA      HPRD    PubMed
 
  NP_001447.1   Glutamate receptor, ionotropic kainate 1   GRIK1      HPRD    PubMed
 
  NP_001447.1   Glutamate receptor, ionotropic kainate 3   GRIK3      HPRD    PubMed
 
  NP_001447.1   NP_000836.1   GRM8      HPRD    PubMed
 
  NP_001447.1   Integrin beta 1   ITGB1      HPRD    PubMed
 
  NP_001447.1   Integrin beta-7   ITGB7      HPRD    PubMed
 
  NP_001447.1   MAP2K4   MAP2K4      HPRD    PubMed
 
  NP_001447.1   NP_663304.1   MAP3K7      HPRD    PubMed
 
  NP_001447.1   NP_055908.1   MAP3K7IP2      HPRD    PubMed
 
  NP_001447.1   MAPK14   MAPK14      HPRD    PubMed
 
  NP_001447.1   Myotilin   MYOT      HPRD    PubMed
 
  NP_001447.1   NP_000263.2   NPHP1      HPRD    PubMed
 
  NP_001447.1   NP_005393.2   RALA      HPRD    PubMed
 
  NP_001447.1   RhoA   RHOA      HPRD    PubMed
 
  NP_001447.1   Selectin E   SELE      HPRD    PubMed
 
  NP_001447.1   LNK   SH2B3      HPRD    PubMed
 
  NP_001447.1   NP_077285.2   TNIP2      HPRD    PubMed
 
  NP_001447.1   NP_066961.2   TRAF2      HPRD    PubMed
 
  NP_001447.1   TRIO   TRIO      HPRD    PubMed
The von Hippel-Lindau tumor suppressor protein (pVHL) interacts with FLNA .
  NP_001447.1   NP_000542.1   VHL      BIND    PubMed
 
  NP_001447.1   VHL   VHL      HPRD    PubMed
 
  NP_001447.1   Rac        HPRD    PubMed
 
  NP_001447.1   mGluR4a        HPRD    PubMed
 
  NP_001447.1   mGluR5a        HPRD    PubMed
 
  NP_001447.1   mGluR7a        HPRD    PubMed
 
  NP_001447.1   mGluR8a        HPRD    PubMed
Two-hybrid
  BioGRID:108605   BioGRID:106862   AR      BioGRID    PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
  BioGRID:108605   BioGRID:107142   BRCA2      BioGRID    PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
  BioGRID:108605   BioGRID:107296   CASR      BioGRID    PubMed
Affinity Capture-Western; Two-hybrid
  BioGRID:108605   BioGRID:123313   CMIP      BioGRID    PubMed
Reconstituted Complex
  BioGRID:108605   BioGRID:108002   DCN      BioGRID    PubMed
Affinity Capture-Western
  BioGRID:108605   BioGRID:108147   DRD2      BioGRID    PubMed
Two-hybrid
  BioGRID:108605   BioGRID:108148   DRD3      BioGRID    PubMed
Reconstituted Complex
  BioGRID:108605   BioGRID:108451   F3      BioGRID    PubMed
Affinity Capture-Western; Two-hybrid
  BioGRID:108605   BioGRID:120128   FBLIM1      BioGRID    PubMed
Affinity Capture-Western; Two-hybrid
  BioGRID:108605   BioGRID:118029   FILIP1      BioGRID    PubMed
Affinity Capture-Western; Two-hybrid
  BioGRID:108605   BioGRID:108606   FLNB      BioGRID    PubMed
Affinity Capture-Western
  BioGRID:108605   BioGRID:109073   GP1BA      BioGRID    PubMed
Reconstituted Complex
  BioGRID:108605   BioGRID:249569   Grm7      BioGRID    PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
  BioGRID:108605   BioGRID:109894   ITGB1      BioGRID    PubMed
Two-hybrid
  BioGRID:108605   BioGRID:109896   ITGB3      BioGRID    PubMed
Two-hybrid
  BioGRID:108605   BioGRID:109900   ITGB6      BioGRID    PubMed
Reconstituted Complex
  BioGRID:108605   BioGRID:109901   ITGB7      BioGRID    PubMed
Affinity Capture-Western
  BioGRID:108605   BioGRID:114878   MYOT      BioGRID    PubMed
Affinity Capture-Western; Two-hybrid
  BioGRID:108605   BioGRID:110927   NPHP1      BioGRID    PubMed
Affinity Capture-Western; Reconstituted Complex
  BioGRID:108605   BioGRID:111834   RALA      BioGRID    PubMed
Affinity Capture-Western; Two-hybrid
  BioGRID:108605   BioGRID:115336   SH2B3      BioGRID    PubMed
Affinity Capture-Western
  BioGRID:108605   BioGRID:113038   TRAF2      BioGRID    PubMed
Reconstituted Complex; Two-hybrid
  BioGRID:108605   BioGRID:113055   TRIO      BioGRID    PubMed
Two-hybrid
  BioGRID:108605   BioGRID:113269   VHL      BioGRID    PubMed

[Top][Help]General gene information

Markers

ECD00755(e-PCR)
Links: UniSTS:281864
ECD02821(e-PCR)
Links: UniSTS:283914
ECD02315(e-PCR)
Links: UniSTS:283415
ECD01291(e-PCR)
Links: UniSTS:282397
ECD01813(e-PCR)
Links: UniSTS:282914
ECD02343(e-PCR)
Links: UniSTS:283442
ECD02344(e-PCR)
Links: UniSTS:283443
ECD00293(e-PCR)
Links: UniSTS:281406
ECD02624(e-PCR)
Links: UniSTS:283718
ECD03921(e-PCR)
Links: UniSTS:285001
MARC_6567-6568:992007312:1(e-PCR)
Links: UniSTS:231246
ECD01863(e-PCR)
Links: UniSTS:282964
REN89250(e-PCR)
Links: UniSTS:414048
ECD02131(e-PCR)
Links: UniSTS:283232
REN89251(e-PCR)
Links: UniSTS:414049
REN89252(e-PCR)
Links: UniSTS:414050
REN89253(e-PCR)
Links: UniSTS:414051
ECD02393(e-PCR)
Links: UniSTS:283491
ECD01622(e-PCR)
Links: UniSTS:282724
REN89254(e-PCR)
Links: UniSTS:414052
ECD02394(e-PCR)
Links: UniSTS:283492
REN89255(e-PCR)
Links: UniSTS:414053
REN89256(e-PCR)
Links: UniSTS:414054
REN89257(e-PCR)
Links: UniSTS:414055
REN89258(e-PCR)
Links: UniSTS:414056
REN89259(e-PCR)
Links: UniSTS:414057
REN89260(e-PCR)
Links: UniSTS:414058
REN89261(e-PCR)
Links: UniSTS:414059
ECD07049(e-PCR)
Links: UniSTS:288107
REN89262(e-PCR)
Links: UniSTS:414060
REN89263(e-PCR)
Links: UniSTS:414061
REN89264(e-PCR)
Links: UniSTS:414062
REN89265(e-PCR)
Links: UniSTS:414063
REN89266(e-PCR)
Links: UniSTS:414064
REN89267(e-PCR)
Links: UniSTS:414065
REN89268(e-PCR)
Links: UniSTS:414066
REN89269(e-PCR)
Links: UniSTS:414067
REN89270(e-PCR)
Links: UniSTS:414068
REN89271(e-PCR)
Links: UniSTS:414069
REN89272(e-PCR)
Links: UniSTS:414070
REN89273(e-PCR)
Links: UniSTS:414071
REN89274(e-PCR)
Links: UniSTS:414072
REN89275(e-PCR)
Links: UniSTS:414073
REN89276(e-PCR)
Links: UniSTS:414074
REN89277(e-PCR)
Links: UniSTS:414075
ECD01647(e-PCR)
Links: UniSTS:282748
REN89278(e-PCR)
Links: UniSTS:414076
REN89279(e-PCR)
Links: UniSTS:414077
REN89280(e-PCR)
Links: UniSTS:414078
ECD02420(e-PCR)
Links: UniSTS:283518
REN89281(e-PCR)
Links: UniSTS:414079
REN89282(e-PCR)
Links: UniSTS:414080
REN89283(e-PCR)
Links: UniSTS:414081
REN89284(e-PCR)
Links: UniSTS:414082
REN89285(e-PCR)
Links: UniSTS:414083
REN89286(e-PCR)
Links: UniSTS:414084
REN89287(e-PCR)
Links: UniSTS:414085
ECD03208(e-PCR)
Links: UniSTS:284293
REN89288(e-PCR)
Links: UniSTS:414086
ECD03209(e-PCR)
Links: UniSTS:284294
REN89289(e-PCR)
Links: UniSTS:414087
REN89290(e-PCR)
Links: UniSTS:414088
REN89291(e-PCR)
Links: UniSTS:414089
REN89292(e-PCR)
Links: UniSTS:414090
REN89293(e-PCR)
Links: UniSTS:414091
ECD12996(e-PCR)
Links: UniSTS:294027
REN89294(e-PCR)
Links: UniSTS:414092
stSG603978(e-PCR)
Links: UniSTS:447372
ECD01664(e-PCR)
Links: UniSTS:282765
REN89295(e-PCR)
Links: UniSTS:414093
stSG603979(e-PCR)
Links: UniSTS:447373
REN89296(e-PCR)
Links: UniSTS:414094
stSG603980(e-PCR)
Links: UniSTS:447374
REN89297(e-PCR)
Links: UniSTS:414095
stSG603981(e-PCR)
Links: UniSTS:447375
REN89298(e-PCR)
Links: UniSTS:414096
stSG603982(e-PCR)
Links: UniSTS:447376
REN89299(e-PCR)
Links: UniSTS:414097
stSG603983(e-PCR)
Links: UniSTS:447377
REN89300(e-PCR)
Links: UniSTS:414098
stSG603984(e-PCR)
Links: UniSTS:447378
REN89301(e-PCR)
Links: UniSTS:414099
stSG603985(e-PCR)
Links: UniSTS:447379
REN89302(e-PCR)
Links: UniSTS:414100
stSG603986(e-PCR)
Links: UniSTS:447380
REN89303(e-PCR)
Links: UniSTS:414101
stSG603987(e-PCR)
Links: UniSTS:447381
REN89304(e-PCR)
Links: UniSTS:414102
stSG603988(e-PCR)
Links: UniSTS:447382
REN89305(e-PCR)
Links: UniSTS:414103
stSG603989(e-PCR)
Links: UniSTS:447383
REN89306(e-PCR)
Links: UniSTS:414104
stSG603991(e-PCR)
Links: UniSTS:447384
REN89307(e-PCR)
Links: UniSTS:414105
stSG603992(e-PCR)
Links: UniSTS:447385
REN89308(e-PCR)
Links: UniSTS:414106
stSG603993(e-PCR)
Links: UniSTS:447386
REN89309(e-PCR)
Links: UniSTS:414107
stSG603997(e-PCR)
Links: UniSTS:447387
REN89310(e-PCR)
Links: UniSTS:414108
REN89311(e-PCR)
Links: UniSTS:414109
REN89312(e-PCR)
Links: UniSTS:414110
REN89313(e-PCR)
Links: UniSTS:414111
REN89314(e-PCR)
Links: UniSTS:414112
REN89315(e-PCR)
Links: UniSTS:414113
REN89316(e-PCR)
Links: UniSTS:414114
REN89317(e-PCR)
Links: UniSTS:414115
REN89318(e-PCR)
Links: UniSTS:414116
DXS1262(e-PCR)
Links: UniSTS:148645
REN89319(e-PCR)
Links: UniSTS:414117
REN89320(e-PCR)
Links: UniSTS:414118
REN89321(e-PCR)
Links: UniSTS:414119
REN89322(e-PCR)
Links: UniSTS:414120
REN89323(e-PCR)
Links: UniSTS:414121
REN89324(e-PCR)
Links: UniSTS:414122
REN89325(e-PCR)
Links: UniSTS:414123
REN89326(e-PCR)
Links: UniSTS:414124
REN89327(e-PCR)
Links: UniSTS:414125
REN89328(e-PCR)
Links: UniSTS:414126
REN89329(e-PCR)
Links: UniSTS:414127
REN89330(e-PCR)
Links: UniSTS:414128
REN89331(e-PCR)
Links: UniSTS:414129
REN89332(e-PCR)
Links: UniSTS:414130
REN89333(e-PCR)
Links: UniSTS:414131
REN89334(e-PCR)
Links: UniSTS:414132
REN89335(e-PCR)
Links: UniSTS:414133
REN89336(e-PCR)
Links: UniSTS:414134
REN89337(e-PCR)
Links: UniSTS:414135
REN89338(e-PCR)
Links: UniSTS:414136
REN89339(e-PCR)
Links: UniSTS:414137
REN89340(e-PCR)
Links: UniSTS:414138
REN89341(e-PCR)
Links: UniSTS:414139
REN89342(e-PCR)
Links: UniSTS:414140
REN89343(e-PCR)
Links: UniSTS:414141
REN89344(e-PCR)
Links: UniSTS:414142
REN89345(e-PCR)
Links: UniSTS:414143
REN89346(e-PCR)
Links: UniSTS:414144
REN89347(e-PCR)
Links: UniSTS:414145
REN89348(e-PCR)
Links: UniSTS:414146
REN89349(e-PCR)
Links: UniSTS:414147
REN89350(e-PCR)
Links: UniSTS:414148
REN89351(e-PCR)
Links: UniSTS:414149
REN89352(e-PCR)
Links: UniSTS:414150
REN89353(e-PCR)
Links: UniSTS:414151
REN89354(e-PCR)
Links: UniSTS:414152
REN89355(e-PCR)
Links: UniSTS:414153
REN89356(e-PCR)
Links: UniSTS:414154
REN89357(e-PCR)
Links: UniSTS:414155
REN89358(e-PCR)
Links: UniSTS:414156
REN89359(e-PCR)
Links: UniSTS:414157
REN89360(e-PCR)
Links: UniSTS:414158
ECD04574(e-PCR)
Links: UniSTS:285646
REN89361(e-PCR)
Links: UniSTS:414159
REN89362(e-PCR)
Links: UniSTS:414160
ECD01732(e-PCR)
Links: UniSTS:282833
REN89363(e-PCR)
Links: UniSTS:414161
ECD05610(e-PCR)
Links: UniSTS:286673
REN89364(e-PCR)
Links: UniSTS:414162
REN89365(e-PCR)
Links: UniSTS:414163
REN89366(e-PCR)
Links: UniSTS:414164
REN89367(e-PCR)
Links: UniSTS:414165
ECD03805(e-PCR)
Links: UniSTS:284885
REN89368(e-PCR)
Links: UniSTS:414166
REN89369(e-PCR)
Links: UniSTS:414167
REN89370(e-PCR)
Links: UniSTS:414168
REN89371(e-PCR)
Links: UniSTS:414169
REN89372(e-PCR)
Links: UniSTS:414170
ECD00453(e-PCR)
Links: UniSTS:281564
GDB:452893(e-PCR)
Links: UniSTS:99294
ECD02527(e-PCR)
Links: UniSTS:283622

Phenotypes

FG syndrome 2
MIM: 300321
Frontometaphyseal dysplasia
MIM: 304120
Frontometaphyseal dysplasia
MIM: 305620
Heterotopia, periventricular
MIM: 300049
Heterotopia, periventricular nodular, with frontometaphyseal dysplasia
MIM: 300049
Heterotopia, periventricular, ED variant
MIM: 300537
Intestinal pseudoobstruction, neuronal
MIM: 300048
Melnick-Needles syndrome
MIM: 309350
Otopalatodigital syndrome, type I
MIM: 311300
Otopalatodigital syndrome, type II
MIM: 304120

Genotypes

See FLNA SNP Genotype Report
See FLNA SNP Geneview Report
See FLNA SNP Variation Viewer Report Variation View Link

Homology

Homologs of the FLNA gene The FLNA gene is conserved in dog, cow, mouse, and rat.


Map Viewer (Mouse, Rat)

Pathways

KEGG pathway: Focal adhesion
04510
KEGG pathway: MAPK signaling pathway
04010
Reactome Event:Hemostasis
REACT_604

[Top][Help]General protein information

Preferred Names
filamin A, alpha
Names
filamin A, alpha
filamin 1
non-muscle filamin
actin binding protein 280
endothelial actin-binding protein

[Top][Help]NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

Genomic

  1. NG_011506.1 RefSeqGene

    Range
    5000..31106
    Download
    GenBank FASTA Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001110556.1NP_001104026.1  filamin A, alpha isoform 2

    Description
    Transcript Variant: This variant (2) includes an alternate in-frame exon and encodes a slightly longer protein isoform (2).
    Source sequence(s)
    AB191260,BC067111,BP235228,X53416
    Consensus CDS
    CCDS48194.1
    UniProtKB/Swiss-Prot
    P21333
    UniProtKB/TrEMBL
    Q5HY55
    UniProtKB/TrEMBL
    Q60FE5
    UniProtKB/TrEMBL
    Q6NXF2
    Conserved Domains (2) summary
    cd00014
    Location:44148
    Blast Score: 254
    CH; Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like...
    cl02665
    Location:18631949
    Blast Score: 304
    Filamin; Filamin/ABP280 repeat
  2. NM_001456.3NP_001447.2  filamin A, alpha isoform 1

    Description
    Transcript Variant: This variant (1) is the predominant transcript and encodes a slightly shorter protein isoform (1).
    Source sequence(s)
    AB191260,BC067111,BP235228,X53416
    Consensus CDS
    CCDS44021.1
    UniProtKB/Swiss-Prot
    P21333
    UniProtKB/TrEMBL
    Q5HY53
    UniProtKB/TrEMBL
    Q60FE5
    UniProtKB/TrEMBL
    Q6NXF2
    Conserved Domains (2) summary
    cd00014
    Location:44148
    Blast Score: 254
    CH; Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like...
    cl02665
    Location:18551941
    Blast Score: 304
    Filamin; Filamin/ABP280 repeat

RefSeqs of Annotated Genomes: Build 37.1

The following sections contain reference sequences that belong to a specific genome build. Explain

Genome Reference Consortium Human Build 37 (GRCh37), Primary_Assembly

Genomic

  1. NC_000023.10

    Range
    153576899..153603005, complement
    Download
    GenBank FASTA Sequence Viewer (Graphics)
  2. NT_167198.1 

    Range
    4494837..4520943, complement
    Download
    GenBank FASTA Sequence Viewer (Graphics)

Alternate assembly (Celera)

Genomic

  1. AC_000066.1

    Range
    153737961..153764067, complement
    Download
    GenBank FASTA Sequence Viewer (Graphics)
  2. NW_927732.1 

    Range
    1445608..1471714, complement
    Download
    GenBank FASTA Sequence Viewer (Graphics)

Alternate assembly (HuRef)

Genomic

  1. AC_000155.1

    Range
    142154186..142180218
    Download
    GenBank FASTA Sequence Viewer (Graphics)
  2. NW_001842419.2 

    Range
    179534..205566
    Download
    GenBank FASTA Sequence Viewer (Graphics)

[Top][Help]Related Sequences

  Nucleotide   Protein
  genomic   BX664723.2   CAI43197.1
       CAI43198.1
       CAI43199.1
       CAI43200.2
       CAI43201.1
  genomic   BX664723.2   CAI43197.1
       CAI43198.1
       CAI43199.1
       CAI43200.2
       CAI43201.1
  genomic   BX936346.4   CAI43225.1
       CAI43226.1
       CAI43227.1
  genomic   CH471172.2   EAW72744.1
       EAW72745.1
       EAW72746.1
       EAW72747.1
       EAW72748.1
  genomic   L44140.1   AAA92644.1
  genomic   X70085.1   CAA49690.1
  mRNA   AB191259.1   BAD52435.1
  mRNA   AB191260.1   BAD52436.1
  mRNA   AB371574.1   BAG48303.1
  mRNA   AB371575.1   BAG48304.1
  mRNA   AB371576.1   BAG48305.1
  mRNA   AB371577.1   BAG48306.1
  mRNA   AB371578.1   BAG48307.1
  mRNA   AB371579.1   BAG48308.1
  mRNA   AK074048.1   BAB84874.1
  mRNA   AK090427.2   BAC03408.2
  mRNA   AK300165.1   BAG61947.1
  mRNA   AK304255.1   BAG65121.1
  mRNA   AL050396.1   None
  mRNA   AL157419.1   None
  mRNA   BC014654.1   AAH14654.1
  mRNA   BC028089.1   None
  mRNA   BC041179.1   AAH41179.1
  mRNA   BC067111.1   AAH67111.1
  mRNA   BC109289.1   AAI09290.3
  mRNA   BP235228.1   None
  mRNA   CR608106.1   None
  mRNA   CR614119.1   None
  mRNA   CR625058.1   None
  mRNA   X53416.1   CAA37495.1
Protein Accession   Links
P21333.4   GenPept   UniProtKB/Swiss-Prot:P21333
Q2VP91   GenPept   UniProtKB/TrEMBL:Q2VP91
Q5HY53   GenPept   UniProtKB/TrEMBL:Q5HY53
Q5HY54   GenPept   UniProtKB/TrEMBL:Q5HY54
Q5HY55   GenPept   UniProtKB/TrEMBL:Q5HY55
Q60FE5   GenPept   UniProtKB/TrEMBL:Q60FE5
Q60FE6   GenPept   UniProtKB/TrEMBL:Q60FE6
Q6NXF2   GenPept   UniProtKB/TrEMBL:Q6NXF2
Q86TQ3   GenPept   UniProtKB/TrEMBL:Q86TQ3
Q8TES4   GenPept   UniProtKB/TrEMBL:Q8TES4
Q96C61   GenPept   UniProtKB/TrEMBL:Q96C61

[Top][Help]Additional Links