Flna (filamin A) - Rat Genome Database

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Gene: Flna (filamin A) Rattus norvegicus
Analyze
Symbol: Flna
Name: filamin A
RGD ID: 1560614
Description: Enables SMAD binding activity. Involved in several processes, including brain development; establishment of Sertoli cell barrier; and mRNA transcription by RNA polymerase II. Located in several cellular components, including cytoskeleton; dendrite; and neuronal cell body. Is active in glutamatergic synapse and postsynapse. Colocalizes with actin filament. Used to study periventricular nodular heterotopia. Human ortholog(s) of this gene implicated in X-linked chronic idiopathic intestinal pseudo-obstruction; bone development disease (multiple); heart valve disease (multiple); periventricular nodular heterotopia; and terminal osseous dysplasia. Orthologous to human FLNA (filamin A); PARTICIPATES IN calcium signaling pathway via the calcium-sensing receptor; integrin mediated signaling pathway; Rho/Rac/Cdc42 mediated signaling pathway; INTERACTS WITH 1-naphthyl isothiocyanate; 17beta-estradiol; 2,3,7,8-tetrachlorodibenzodioxine.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: actin binding protein 280; Endothelial actin-binding protein 280); filamin A, alpha; filamin, alpha; filamin-A; LOC293860; RGD1560614; similar to Filamin A (Alpha-filamin) (Filamin 1) (Endothelial actin-binding protein) (Actin-binding protein 280) (ABP-280) (Nonmuscle filamin); similar to Filamin A (Alpha-filamin, Endothelial actin-binding protein 280)
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Allele / Splice: Flnaem1Ang  
Genetic Models: SD-Flnaem1Ang
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr8X157,159,051 - 157,185,559 (-)NCBIGRCr8
mRatBN7.2X152,007,758 - 152,034,266 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 EnsemblX152,007,758 - 152,031,052 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_UtxX154,148,888 - 154,172,182 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0X157,712,123 - 157,735,417 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0X155,383,921 - 155,407,213 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0X156,460,785 - 156,487,245 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 EnsemblX156,463,953 - 156,487,245 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.01152,200,936 - 152,227,391 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4X160,362,334 - 160,385,626 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
Celera1135,865,679 - 135,888,971 (+)NCBICelera
Cytogenetic MapXq37NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Disease Annotations     Click to see Annotation Detail View
adrenoleukodystrophy  (ISO)
Aneurysm  (ISO)
aortic aneurysm  (ISO)
Arterial Thrombosis  (ISO)
arterial tortuosity syndrome  (ISO)
autistic disorder  (ISO)
Barth syndrome  (ISO)
Breast Neoplasms  (ISO)
cerebral creatine deficiency syndrome 1  (ISO)
cleft palate  (ISO)
colitis  (ISO)
congenital heart disease  (ISO)
connective tissue disease  (ISO)
craniosynostosis  (ISO)
Developmental Disabilities  (ISO)
disorder of sexual development  (ISO)
Dwarfism  (ISO)
dyskeratosis congenita  (ISO)
Ehlers-Danlos syndrome  (ISO)
Ehlers-Danlos syndrome classic type 1  (ISO)
Emery-Dreifuss muscular dystrophy  (ISO)
epilepsy  (ISO)
Experimental Liver Cirrhosis  (ISO)
Familial Sudden Death  (ISO)
Familial Thoracic Aortic Aneurysm 2  (ISO)
favism  (ISO)
FG syndrome  (ISO)
FG Syndrome 2  (ISO)
frontometaphyseal dysplasia  (ISO)
frontometaphyseal dysplasia 1  (ISO)
Gastrointestinal Hemorrhage  (ISO)
genetic disease  (ISO)
hemorrhagic disease  (ISO)
hepatoblastoma  (ISO)
hereditary breast ovarian cancer syndrome  (ISO)
hydronephrosis  (ISO)
immunodeficiency 33  (ISO)
intellectual disability  (ISO)
Juberg Hayward Syndrome  (ISO)
lung disease  (ISO)
Marfan syndrome  (ISO)
Melnick-Needles syndrome  (ISO)
methylmalonic acidemia and homocysteinemia cblX type  (ISO)
microcephaly  (ISO)
mitral valve prolapse  (ISO)
Muscle Hypotonia  (ISO)
myopia  (ISO)
NEURODEVELOPMENTAL DISORDER WITH MICROCEPHALY, ARTHROGRYPOSIS, AND STRUCTURAL BRAIN ANOMALIES  (ISO)
Neurodevelopmental Disorders  (ISO)
Nijmegen breakage syndrome  (ISO)
omphalocele  (ISO)
orofacial cleft  (ISO)
osteochondrodysplasia  (ISO)
otopalatodigital syndrome spectrum disorder  (ISO)
otopalatodigital syndrome type 1  (ISO)
otopalatodigital syndrome type 2  (ISO)
paraplegia  (ISO)
patent foramen ovale  (ISO)
periventricular nodular heterotopia  (IMP,ISO,ISS)
Periventricular Nodular Heterotopia 4  (ISO)
Phyllodes Tumor  (ISO)
prune belly syndrome  (ISO)
scoliosis  (ISO)
severe congenital encephalopathy due to MECP2 mutation  (ISO)
Splenomegaly  (ISO)
Stroke  (ISO)
syndromic X-linked intellectual disability Lubs type  (ISO)
terminal osseous dysplasia  (ISO)
thoracic aortic aneurysm  (ISO)
thrombocytopenia  (ISO)
tuberous sclerosis  (ISO)
ventricular septal defect  (ISO)
Wolff-Parkinson-White syndrome  (ISO)
X-linked cardiac valvular dysplasia  (ISO)
X-linked chronic idiopathic intestinal pseudo-obstruction  (ISO)

Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(-)-epigallocatechin 3-gallate  (ISO)
1,1-dichloroethene  (ISO)
1,2-dimethylhydrazine  (ISO)
1-chloro-2,4-dinitrobenzene  (ISO)
1-naphthyl isothiocyanate  (EXP)
17alpha-ethynylestradiol  (ISO)
17beta-estradiol  (EXP,ISO)
2,2',4,4',5,5'-hexachlorobiphenyl  (ISO)
2,2',5,5'-tetrachlorobiphenyl  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,3,7,8-Tetrachlorodibenzofuran  (EXP)
2-palmitoylglycerol  (ISO)
3,4-methylenedioxymethamphetamine  (ISO)
4,4'-diaminodiphenylmethane  (EXP)
4,4'-sulfonyldiphenol  (ISO)
4-hydroxyphenyl retinamide  (ISO)
5-aza-2'-deoxycytidine  (ISO)
acetamide  (EXP)
acrolein  (ISO)
afimoxifene  (ISO)
aflatoxin B1  (ISO)
Aflatoxin B2 alpha  (ISO)
all-trans-retinoic acid  (ISO)
antimycin A  (ISO)
Aroclor 1254  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
arsenic trichloride  (ISO)
arsenite(3-)  (ISO)
artesunate  (ISO)
atrazine  (ISO)
benzene  (ISO)
benzo[a]pyrene  (ISO)
benzo[e]pyrene  (ISO)
bis(2-ethylhexyl) phthalate  (ISO)
bisphenol A  (EXP,ISO)
Bisphenol B  (ISO)
bisphenol F  (ISO)
cadmium atom  (ISO)
cadmium dichloride  (ISO)
caffeine  (ISO)
captan  (ISO)
carbon nanotube  (ISO)
CGP 52608  (ISO)
chlordecone  (ISO)
cisplatin  (ISO)
clofibrate  (ISO)
cobalt dichloride  (ISO)
copper atom  (ISO)
copper(0)  (ISO)
copper(II) sulfate  (ISO)
coumarin  (ISO)
crocidolite asbestos  (ISO)
Cuprizon  (EXP)
cyclosporin A  (ISO)
deguelin  (ISO)
deoxynivalenol  (ISO)
dextran sulfate  (ISO)
dibutyl phthalate  (EXP,ISO)
dichloroacetic acid  (ISO)
dicrotophos  (ISO)
dihydroartemisinin  (ISO)
diuron  (EXP)
dorsomorphin  (ISO)
doxorubicin  (ISO)
elemental selenium  (ISO)
ellagic acid  (ISO)
enzyme inhibitor  (ISO)
epoxiconazole  (ISO)
ethanol  (ISO)
fenamidone  (ISO)
flutamide  (EXP)
folic acid  (ISO)
folpet  (ISO)
FR900359  (ISO)
genistein  (ISO)
glafenine  (EXP)
glyphosate  (ISO)
graphite  (ISO)
hydrogen peroxide  (ISO)
inulin  (ISO)
iron dichloride  (ISO)
isotretinoin  (ISO)
ivermectin  (ISO)
lead(0)  (ISO)
levofloxacin  (EXP)
lipopolysaccharide  (ISO)
methamphetamine  (ISO)
methapyrilene  (ISO)
N-acetyl-L-cysteine  (ISO)
N-nitrosodimethylamine  (EXP)
nickel sulfate  (ISO)
nitrofen  (EXP)
ozone  (ISO)
paracetamol  (ISO)
PCB138  (ISO)
pentanal  (ISO)
perfluorooctane-1-sulfonic acid  (ISO)
phenethyl isothiocyanate  (EXP)
phenylmercury acetate  (ISO)
picoxystrobin  (ISO)
potassium chromate  (ISO)
propanal  (ISO)
quercetin  (ISO)
rotenone  (ISO)
SB 431542  (ISO)
selenium atom  (ISO)
silicon dioxide  (ISO)
sodium arsenite  (EXP,ISO)
sodium dichromate  (ISO)
tebuconazole  (ISO)
tebufenpyrad  (ISO)
temozolomide  (ISO)
tetrachloromethane  (ISO)
thifluzamide  (ISO)
toluene  (ISO)
triphenylstannane  (ISO)
triptonide  (ISO)
tungsten  (ISO)
urethane  (ISO)
valproic acid  (ISO)
vancomycin  (ISO)
vinclozolin  (EXP)
vitamin E  (ISO)
wortmannin  (ISO)
xylitol  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Biological Process
actin crosslink formation  (ISO)
actin cytoskeleton organization  (ISO)
adenylate cyclase-inhibiting dopamine receptor signaling pathway  (ISO)
angiogenesis  (ISO)
blood vessel remodeling  (ISO)
cell-cell junction organization  (ISO)
cerebral cortex development  (IEP)
cilium assembly  (ISO)
cytoplasmic sequestering of protein  (ISO)
early endosome to late endosome transport  (ISO)
epithelial to mesenchymal transition  (ISO)
establishment of protein localization  (ISO)
establishment of Sertoli cell barrier  (IMP)
formation of radial glial scaffolds  (IMP)
heart morphogenesis  (ISO)
mitotic spindle assembly  (ISO)
mRNA transcription by RNA polymerase II  (IMP)
negative regulation of apoptotic process  (ISO)
negative regulation of neuron projection development  (ISO)
negative regulation of protein catabolic process  (ISO)
negative regulation of transcription by RNA polymerase I  (ISO)
platelet aggregation  (ISO)
positive regulation of actin filament bundle assembly  (IMP)
positive regulation of axon regeneration  (ISO)
positive regulation of canonical NF-kappaB signal transduction  (ISO)
positive regulation of integrin-mediated signaling pathway  (ISO)
positive regulation of neural precursor cell proliferation  (IMP)
positive regulation of neuron migration  (IMP)
positive regulation of potassium ion transmembrane transport  (ISO)
positive regulation of protein import into nucleus  (ISO)
positive regulation of substrate adhesion-dependent cell spreading  (ISO)
protein localization to bicellular tight junction  (IMP)
protein localization to cell surface  (ISO)
protein localization to plasma membrane  (ISO)
protein stabilization  (ISO)
receptor clustering  (ISO)
regulation of actin filament bundle assembly  (ISO)
regulation of cell migration  (ISO)
regulation of membrane repolarization during cardiac muscle cell action potential  (ISO)
semaphorin-plexin signaling pathway  (ISO)
synapse organization  (ISO)
wound healing, spreading of cells  (ISO)

References

References - curated
# Reference Title Reference Citation
1. Screening of TGFBR1, TGFBR2, and FLNA in familial mitral valve prolapse. Aalberts JJ, etal., Am J Med Genet A. 2014 Jan;164A(1):113-9. doi: 10.1002/ajmg.a.36211. Epub 2013 Nov 15.
2. Insulin-like growth factor-binding protein-5-induced laminin gamma1 transcription requires filamin A. Abrass CK and Hansen KM, J Biol Chem. 2010 Apr 23;285(17):12925-34. doi: 10.1074/jbc.M109.061754. Epub 2010 Feb 18.
3. Integrin inactivators: balancing cellular functions in vitro and in vivo. Bouvard D, etal., Nat Rev Mol Cell Biol. 2013 Jul;14(7):430-42. doi: 10.1038/nrm3599. Epub 2013 May 30.
4. A glial origin for periventricular nodular heterotopia caused by impaired expression of Filamin-A. Carabalona A, etal., Hum Mol Genet. 2012 Mar 1;21(5):1004-17. doi: 10.1093/hmg/ddr531. Epub 2011 Nov 10.
5. Association of mutations in FLNA with craniosynostosis. Fennell N, etal., Eur J Hum Genet. 2015 Dec;23(12):1684-8. doi: 10.1038/ejhg.2015.31. Epub 2015 Apr 15.
6. Mutations in filamin 1 prevent migration of cerebral cortical neurons in human periventricular heterotopia. Fox JW, etal., Neuron. 1998 Dec;21(6):1315-25.
7. Astrocytic inclusions in epilepsy: expanding the spectrum of filaminopathies. Hazrati LN, etal., J Neuropathol Exp Neurol. 2008 Jul;67(7):669-76. doi: 10.1097/NEN.0b013e31817d7a06.
8. Mutations in the gene encoding filamin A as a cause for familial cardiac valvular dystrophy. Kyndt F, etal., Circulation. 2007 Jan 2;115(1):40-9. Epub 2006 Dec 26.
9. Dynamic interactions of Fc gamma receptor IIB with filamin-bound SHIP1 amplify filamentous actin-dependent negative regulation of Fc epsilon receptor I signaling. Lesourne R, etal., J Immunol. 2005 Feb 1;174(3):1365-73.
10. Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling. Nakamura F, etal., Nat Commun. 2014 Oct 31;5:5325. doi: 10.1038/ncomms6325.
11. Distinct regional and subcellular localization of the actin-binding protein filamin A in the mature rat brain. Noam Y, etal., J Comp Neurol. 2012 Sep 1;520(13):3013-34. doi: 10.1002/cne.23106.
12. Novel no-stop FLNA mutation causes multi-organ involvement in males. Oegema R, etal., Am J Med Genet A. 2013 Sep;161A(9):2376-84. doi: 10.1002/ajmg.a.36109. Epub 2013 Jul 19.
13. OMIM Disease Annotation Pipeline OMIM Disease Annotation Pipeline
14. Familial periventricular nodular heterotopia, epilepsy and Melnick-Needles Syndrome caused by a single FLNA mutation with combined gain-of-function and loss-of-function effects. Parrini E, etal., J Med Genet. 2015 Jun;52(6):405-12. doi: 10.1136/jmedgenet-2014-102959. Epub 2015 Mar 9.
15. Calcium-sensing receptor activation of rho involves filamin and rho-guanine nucleotide exchange factor. Pi M, etal., Endocrinology. 2002 Oct;143(10):3830-8.
16. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
17. PID Annotation Import Pipeline Pipeline to import Pathway Interaction Database annotations from NCI into RGD
18. HCN1 and HCN2 proteins are expressed in cochlear hair cells: HCN1 can form a ternary complex with protocadherin 15 CD3 and F-actin-binding filamin A or can interact with HCN2. Ramakrishnan NA, etal., J Biol Chem. 2012 Nov 2;287(45):37628-46. doi: 10.1074/jbc.M112.375832. Epub 2012 Sep 4.
19. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
20. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
21. Comprehensive gene review and curation RGD comprehensive gene curation
22. Frontometaphyseal dysplasia: mutations in FLNA and phenotypic diversity. Robertson SP, etal., Am J Med Genet A. 2006 Aug 15;140(16):1726-36.
23. Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans. Robertson SP, etal., Nat Genet. 2003 Apr;33(4):487-91. Epub 2003 Mar 3.
24. The Oxygen Sensor PHD2 Controls Dendritic Spines and Synapses via Modification of Filamin A. Segura I, etal., Cell Rep. 2016 Mar 22;14(11):2653-67. doi: 10.1016/j.celrep.2016.02.047. Epub 2016 Mar 10.
25. Mutations in the X-linked filamin 1 gene cause periventricular nodular heterotopia in males as well as in females. Sheen VL, etal., Hum Mol Genet. 2001 Aug 15;10(17):1775-83.
26. A novel 9 bp deletion in the filamin a gene causes an otopalatodigital-spectrum disorder with a variable, intermediate phenotype. Stefanova M, etal., Am J Med Genet A. 2005 Feb 1;132A(4):386-90.
27. Filamin A is a regulator of blood-testis barrier assembly during postnatal development in the rat testis. Su W, etal., Endocrinology. 2012 Oct;153(10):5023-35. Epub 2012 Aug 7.
28. Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and filamin A. Torrado M, etal., Invest Ophthalmol Vis Sci 2004 Nov;45(11):3955-63.
29. Naloxone's pentapeptide binding site on filamin A blocks Mu opioid receptor-Gs coupling and CREB activation of acute morphine. Wang HY and Burns LH, PLoS One. 2009;4(1):e4282. doi: 10.1371/journal.pone.0004282. Epub 2009 Jan 27.
30. MEK-ERK1/2-dependent FLNA overexpression promotes abnormal dendritic patterning in tuberous sclerosis independent of mTOR. Zhang L, etal., Neuron. 2014 Oct 1;84(1):78-91. doi: 10.1016/j.neuron.2014.09.009.
31. Circular RNA expression profile and potential function of hsa_circRNA_101238 in human thoracic aortic dissection. Zou M, etal., Oncotarget. 2017 Jul 5;8(47):81825-81837. doi: 10.18632/oncotarget.18998. eCollection 2017 Oct 10.
Additional References at PubMed
PMID:1833070   PMID:2391361   PMID:3138234   PMID:4044584   PMID:9412467   PMID:10051605   PMID:10692483   PMID:11909861   PMID:12704190   PMID:12761501   PMID:15509752   PMID:15632090  
PMID:15684392   PMID:16291724   PMID:17172441   PMID:17536008   PMID:18177638   PMID:18322202   PMID:18548008   PMID:18555800   PMID:19056867   PMID:19946888   PMID:20458337   PMID:20713593  
PMID:21362503   PMID:21423176   PMID:21478251   PMID:21507248   PMID:21709252   PMID:21914078   PMID:22114352   PMID:22121117   PMID:22307607   PMID:22658674   PMID:22681889   PMID:23106098  
PMID:23376485   PMID:23382103   PMID:23533145   PMID:23979707   PMID:24403084   PMID:24436304   PMID:24828612   PMID:24951510   PMID:25468996   PMID:26157139   PMID:26460884   PMID:35352799  
PMID:37740811  


Genomics

Comparative Map Data
Flna
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr8X157,159,051 - 157,185,559 (-)NCBIGRCr8
mRatBN7.2X152,007,758 - 152,034,266 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 EnsemblX152,007,758 - 152,031,052 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_UtxX154,148,888 - 154,172,182 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0X157,712,123 - 157,735,417 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0X155,383,921 - 155,407,213 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0X156,460,785 - 156,487,245 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 EnsemblX156,463,953 - 156,487,245 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.01152,200,936 - 152,227,391 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4X160,362,334 - 160,385,626 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
Celera1135,865,679 - 135,888,971 (+)NCBICelera
Cytogenetic MapXq37NCBI
FLNA
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh38X154,348,531 - 154,374,634 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 EnsemblX154,348,524 - 154,374,634 (-)EnsemblGRCh38hg38GRCh38
GRCh37X153,576,899 - 153,603,002 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 36X153,230,091 - 153,252,845 (-)NCBINCBI36Build 36hg18NCBI36
Build 34X153,097,811 - 153,123,776NCBI
CeleraX153,737,962 - 153,764,068 (-)NCBICelera
Cytogenetic MapXq28NCBI
HuRefX142,154,186 - 142,180,218 (-)NCBIHuRef
CHM1_1X153,488,516 - 153,514,622 (-)NCBICHM1_1
T2T-CHM13v2.0X152,585,064 - 152,611,166 (-)NCBIT2T-CHM13v2.0
Flna
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm39X73,267,067 - 73,293,787 (-)NCBIGRCm39GRCm39mm39
GRCm39 EnsemblX73,267,067 - 73,293,426 (-)EnsemblGRCm39 Ensembl
GRCm38X74,223,461 - 74,249,854 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 EnsemblX74,223,461 - 74,249,820 (-)EnsemblGRCm38mm10GRCm38
MGSCv37X71,468,800 - 71,491,873 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv36X71,468,800 - 71,491,873 (-)NCBIMGSCv36mm8
CeleraX65,477,570 - 65,500,684 (-)NCBICelera
Cytogenetic MapXA7.3NCBI
cM MapX37.89NCBI
Flna
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_004955580874,233 - 895,232 (+)EnsemblChiLan1.0
ChiLan1.0NW_004955580874,233 - 895,172 (+)NCBIChiLan1.0ChiLan1.0
FLNA
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1-v2X154,331,705 - 154,357,899 (+)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan1X154,335,307 - 154,361,504 (+)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v0X143,799,088 - 143,825,282 (+)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
FLNA
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.1X122,058,303 - 122,083,467 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 EnsemblX122,061,455 - 122,083,203 (+)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_TashaX107,387,038 - 107,412,214 (+)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.0X125,200,002 - 125,225,183 (+)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 EnsemblX125,199,994 - 125,369,947 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1X120,969,062 - 120,994,237 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0X123,484,172 - 123,509,345 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0X123,246,013 - 123,271,198 (+)NCBIUU_Cfam_GSD_1.0
Flna
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2X119,359,521 - 119,385,421 (-)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_0049368091,097,294 - 1,123,201 (-)EnsemblSpeTri2.0SpeTri2.0 Ensembl
SpeTri2.0NW_0049368091,097,288 - 1,123,206 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
FLNA
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 EnsemblX124,890,162 - 124,914,992 (+)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1X124,889,934 - 124,915,000 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
FLNA
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.1X128,657,580 - 128,683,812 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 EnsemblX128,657,393 - 128,680,531 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_02366606566,586,882 - 66,613,103 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Flna
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_004624946812,287 - 837,273 (+)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_004624946812,278 - 836,307 (+)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Flna
5 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:63
Count of miRNA genes:52
Interacting mature miRNAs:62
Transcripts:ENSRNOT00000068489
Prediction methods:Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
10059603Bw174Body weight QTL 1743.40.025body mass (VT:0001259)body weight (CMO:0000012)X113937816152453651Rat
634346Insul4Insulin level QTL 40blood insulin amount (VT:0001560)serum insulin level (CMO:0000358)X126975089152453651Rat

Markers in Region
RH134438  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,007,793 - 152,007,978 (-)MAPPERmRatBN7.2
Rnor_6.0X156,487,025 - 156,487,209NCBIRnor6.0
Rnor_5.01152,227,171 - 152,227,355UniSTSRnor5.0
RGSC_v3.4X160,385,406 - 160,385,590UniSTSRGSC3.4
Celera1135,888,751 - 135,888,935UniSTS
Cytogenetic MapXq37UniSTS
REN89263  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,010,621 - 152,010,861 (-)MAPPERmRatBN7.2
Rnor_6.0X156,484,142 - 156,484,381NCBIRnor6.0
Rnor_5.01152,224,288 - 152,224,527UniSTSRnor5.0
RGSC_v3.4X160,382,523 - 160,382,762UniSTSRGSC3.4
Celera1135,885,868 - 135,886,107UniSTS
Cytogenetic MapXq37UniSTS
REN89262  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,010,389 - 152,010,642 (-)MAPPERmRatBN7.2
Rnor_6.0X156,484,361 - 156,484,613NCBIRnor6.0
Rnor_5.01152,224,507 - 152,224,759UniSTSRnor5.0
RGSC_v3.4X160,382,742 - 160,382,994UniSTSRGSC3.4
Celera1135,886,087 - 135,886,339UniSTS
Cytogenetic MapXq37UniSTS
REN89288  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,016,721 - 152,017,012 (-)MAPPERmRatBN7.2
Rnor_6.0X156,477,991 - 156,478,281NCBIRnor6.0
Rnor_5.01152,218,137 - 152,218,427UniSTSRnor5.0
RGSC_v3.4X160,376,372 - 160,376,662UniSTSRGSC3.4
Celera1135,879,717 - 135,880,007UniSTS
Cytogenetic MapXq37UniSTS
REN89289  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,016,991 - 152,017,219 (-)MAPPERmRatBN7.2
Rnor_6.0X156,477,784 - 156,478,011NCBIRnor6.0
Rnor_5.01152,217,930 - 152,218,157UniSTSRnor5.0
RGSC_v3.4X160,376,165 - 160,376,392UniSTSRGSC3.4
Celera1135,879,510 - 135,879,737UniSTS
Cytogenetic MapXq37UniSTS
REN89318  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,023,459 - 152,023,712 (-)MAPPERmRatBN7.2
Rnor_6.0X156,471,293 - 156,471,545NCBIRnor6.0
Rnor_5.01152,211,439 - 152,211,691UniSTSRnor5.0
RGSC_v3.4X160,369,674 - 160,369,926UniSTSRGSC3.4
Celera1135,873,019 - 135,873,271UniSTS
Cytogenetic MapXq37UniSTS
REN89349  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,030,668 - 152,030,896 (-)MAPPERmRatBN7.2
Rnor_6.0X156,464,109 - 156,464,336NCBIRnor6.0
Rnor_5.01152,204,255 - 152,204,482UniSTSRnor5.0
RGSC_v3.4X160,362,490 - 160,362,717UniSTSRGSC3.4
Celera1135,865,835 - 135,866,062UniSTS
Cytogenetic MapXq37UniSTS
ECD00293  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,026,226 - 152,027,292 (-)MAPPERmRatBN7.2
Rnor_6.0X156,467,713 - 156,468,778NCBIRnor6.0
Rnor_5.01152,207,859 - 152,208,924UniSTSRnor5.0
RGSC_v3.4X160,366,094 - 160,367,159UniSTSRGSC3.4
Celera1135,869,439 - 135,870,504UniSTS
Cytogenetic MapXq37UniSTS
ECD01291  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,024,355 - 152,025,192 (-)MAPPERmRatBN7.2
Rnor_6.0X156,469,813 - 156,470,649NCBIRnor6.0
Rnor_5.01152,209,959 - 152,210,795UniSTSRnor5.0
RGSC_v3.4X160,368,194 - 160,369,030UniSTSRGSC3.4
Celera1135,871,539 - 135,872,375UniSTS
Cytogenetic MapXq37UniSTS
ECD02527  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X152,013,058 - 152,014,219 (-)MAPPERmRatBN7.2
Rnor_6.0X156,480,784 - 156,481,944NCBIRnor6.0
Rnor_5.01152,220,930 - 152,222,090UniSTSRnor5.0
RGSC_v3.4X160,379,165 - 160,380,325UniSTSRGSC3.4
Celera1135,882,510 - 135,883,670UniSTS
Cytogenetic MapXq37UniSTS


Genetic Models
This gene Flna is modified in the following models/strains:


Expression


RNA-SEQ Expression
High: > 1000 TPM value   Medium: Between 11 and 1000 TPM
Low: Between 0.5 and 10 TPM   Below Cutoff: < 0.5 TPM

alimentary part of gastrointestinal system circulatory system endocrine system exocrine system hemolymphoid system hepatobiliary system integumental system musculoskeletal system nervous system renal system reproductive system respiratory system appendage
High 3
Medium 3 43 50 34 19 34 8 11 74 35 37 11 8
Low 7 7 7 1
Below cutoff

Sequence


RefSeq Acc Id: ENSRNOT00000079889   ⟹   ENSRNOP00000070703
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 EnsemblX152,007,758 - 152,031,052 (-)Ensembl
Rnor_6.0 EnsemblX156,463,953 - 156,487,245 (+)Ensembl
RefSeq Acc Id: ENSRNOT00000095996   ⟹   ENSRNOP00000076405
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 EnsemblX152,007,758 - 152,031,052 (-)Ensembl
RefSeq Acc Id: ENSRNOT00000109154   ⟹   ENSRNOP00000082035
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 EnsemblX152,007,781 - 152,030,992 (-)Ensembl
RefSeq Acc Id: ENSRNOT00000118254   ⟹   ENSRNOP00000077541
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 EnsemblX152,007,758 - 152,031,052 (-)Ensembl
RefSeq Acc Id: NM_001134599   ⟹   NP_001128071
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8X157,159,051 - 157,182,343 (-)NCBI
mRatBN7.2X152,007,758 - 152,031,052 (-)NCBI
Rnor_6.0X156,463,953 - 156,487,245 (+)NCBI
Rnor_5.01152,200,936 - 152,227,391 (+)NCBI
RGSC_v3.4X160,362,334 - 160,385,626 (+)RGD
Celera1135,865,679 - 135,888,971 (+)NCBI
Sequence:
RefSeq Acc Id: XM_006229569   ⟹   XP_006229631
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8X157,159,068 - 157,185,559 (-)NCBI
mRatBN7.2X152,007,769 - 152,034,266 (-)NCBI
Rnor_6.0X156,460,785 - 156,487,240 (+)NCBI
Rnor_5.01152,200,936 - 152,227,391 (+)NCBI
Sequence:
RefSeq Acc Id: XM_006229570   ⟹   XP_006229632
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8X157,159,068 - 157,185,559 (-)NCBI
mRatBN7.2X152,007,769 - 152,034,266 (-)NCBI
Rnor_6.0X156,460,785 - 156,487,240 (+)NCBI
Rnor_5.01152,200,936 - 152,227,391 (+)NCBI
Sequence:
RefSeq Acc Id: XM_063279839   ⟹   XP_063135909
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8X157,159,068 - 157,185,501 (-)NCBI
RefSeq Acc Id: XM_063279840   ⟹   XP_063135910
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8X157,159,068 - 157,185,501 (-)NCBI
RefSeq Acc Id: NP_001128071   ⟸   NM_001134599
- UniProtKB: C0JPT7 (UniProtKB/TrEMBL),   A6KRS3 (UniProtKB/TrEMBL),   A6KRS4 (UniProtKB/TrEMBL),   A0A0G2JYL6 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006229631   ⟸   XM_006229569
- Peptide Label: isoform X1
- UniProtKB: A0A8I5ZV49 (UniProtKB/TrEMBL),   A6KRS4 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: XP_006229632   ⟸   XM_006229570
- Peptide Label: isoform X2
- UniProtKB: C0JPT7 (UniProtKB/TrEMBL),   A6KRS3 (UniProtKB/TrEMBL),   A6KRS4 (UniProtKB/TrEMBL),   A0A0G2JYL6 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000070703   ⟸   ENSRNOT00000079889
RefSeq Acc Id: ENSRNOP00000076405   ⟸   ENSRNOT00000095996
RefSeq Acc Id: ENSRNOP00000077541   ⟸   ENSRNOT00000118254
RefSeq Acc Id: ENSRNOP00000082035   ⟸   ENSRNOT00000109154
RefSeq Acc Id: XP_063135910   ⟸   XM_063279840
- Peptide Label: isoform X2
RefSeq Acc Id: XP_063135909   ⟸   XM_063279839
- Peptide Label: isoform X1
Protein Domains
Calponin-homology (CH)

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-C0JPT7-F1-model_v2 AlphaFold C0JPT7 1-2639 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Promoters
RGD ID:13702049
Promoter ID:EPDNEW_R12573
Type:multiple initiation site
Name:Flna_1
Description:filamin A
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
Rat AssemblyChrPosition (strand)Source
Rnor_6.0X156,464,013 - 156,464,073EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:1560614 AgrOrtholog
BioCyc Gene G2FUF-638 BioCyc
Ensembl Genes ENSRNOG00000054890 Ensembl, ENTREZGENE, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000079889 ENTREZGENE
  ENSRNOT00000079889.2 UniProtKB/TrEMBL
  ENSRNOT00000095996.1 UniProtKB/TrEMBL
  ENSRNOT00000109154.1 UniProtKB/TrEMBL
  ENSRNOT00000118254.1 UniProtKB/TrEMBL
Gene3D-CATH 1.10.418.10 UniProtKB/TrEMBL
  2.60.40.10 UniProtKB/TrEMBL
InterPro Actinin_actin-bd_CS UniProtKB/TrEMBL
  Calponin-like_dom_sf UniProtKB/TrEMBL
  Calponin_act-bd UniProtKB/TrEMBL
  Filamin UniProtKB/TrEMBL
  Filamin UniProtKB/TrEMBL
  Filamin/ABP280_repeat-like UniProtKB/TrEMBL
  Ig-like_fold UniProtKB/TrEMBL
  Ig_E-set UniProtKB/TrEMBL
KEGG Report rno:293860 UniProtKB/TrEMBL
NCBI Gene 293860 ENTREZGENE
PANTHER FILAMIN-A UniProtKB/TrEMBL
  PTHR38537 UniProtKB/TrEMBL
Pfam Filamin UniProtKB/TrEMBL
  PF00307 UniProtKB/TrEMBL
PharmGKB FLNA RGD
PhenoGen Flna PhenoGen
PROSITE ACTININ_1 UniProtKB/TrEMBL
  ACTININ_2 UniProtKB/TrEMBL
  FILAMIN_REPEAT UniProtKB/TrEMBL
  PS50021 UniProtKB/TrEMBL
RatGTEx ENSRNOG00000054890 RatGTEx
SMART IG_FLMN UniProtKB/TrEMBL
  SM00033 UniProtKB/TrEMBL
Superfamily-SCOP Calponin-homology UniProtKB/TrEMBL
  Ig_E-set UniProtKB/TrEMBL
UniProt A0A0G2JYL6 ENTREZGENE, UniProtKB/TrEMBL
  A0A8I5Y6H8_RAT UniProtKB/TrEMBL
  A0A8I5Y7V6_RAT UniProtKB/TrEMBL
  A0A8I5ZV49 ENTREZGENE, UniProtKB/TrEMBL
  A6KRS3 ENTREZGENE, UniProtKB/TrEMBL
  A6KRS4 ENTREZGENE, UniProtKB/TrEMBL
  C0JPT7 ENTREZGENE
UniProt Secondary C0JPT7 UniProtKB/TrEMBL


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2016-01-11 Flna  filamin A  Flna  filamin A, alpha  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2010-02-24 Flna  filamin A, alpha  Flna  filamin, alpha   Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2008-04-30 Flna  filamin, alpha   Flna_predicted  filamin, alpha (predicted)  'predicted' is removed 2292626 APPROVED
2006-03-30 Flna_predicted  filamin, alpha (predicted)  RGD1560614_predicted  similar to Filamin A (Alpha-filamin; Endothelial actin-binding protein 280) (predicted)  Symbol and Name updated 1299863 APPROVED
2006-03-10 RGD1560614_predicted  similar to Filamin A (Alpha-filamin; Endothelial actin-binding protein 280) (predicted)    similar to Filamin A (Alpha-filamin) (Filamin 1) (Endothelial actin-binding protein) (Actin-binding protein 280) (ABP-280) (Nonmuscle filamin) (predicted)  Name updated 1299863 APPROVED
2006-03-07 RGD1560614_predicted  similar to Filamin A (Alpha-filamin) (Filamin 1) (Endothelial actin-binding protein) (Actin-binding protein 280) (ABP-280) (Nonmuscle filamin) (predicted)  LOC293860  similar to Filamin A (Alpha-filamin) (Filamin 1) (Endothelial actin-binding protein) (Actin-binding protein 280) (ABP-280) (Nonmuscle filamin)  Symbol and Name status set to approved 1299863 APPROVED
2006-02-09 LOC293860  similar to Filamin A (Alpha-filamin) (Filamin 1) (Endothelial actin-binding protein) (Actin-binding protein 280) (ABP-280) (Nonmuscle filamin)      Symbol and Name status set to provisional 70820 PROVISIONAL