HUMAN:FLNA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FLNA (synonyms: FLN, FLN1)
Protein Name(s)	Filamin-A FLN-A Actin-binding protein 280 ABP-280 Alpha-filamin Endothelial actin-binding protein Filamin-1 Non-muscle filamin
External Links
UniProt	P21333
EMBL	X53416 L44140 X70082 X70085 GU727643 AK090427 AB593010 BX664723 BX936346 BX664723 BX936346 BX936346 BX664723 BX936346 BX664723 CH471172 CH471172
CCDS	CCDS44021.1 CCDS48194.1
PIR	A37098
RefSeq	NP_001104026.1 NP_001447.2
UniGene	Hs.195464
PDB	2AAV 2BP3 2BRQ 2J3S 2JF1 2K3T 2K7P 2K7Q 2W0P 2WFN 3CNK 3HOC 3HOP 3HOR 3ISW 3RGH 4M9P
PDBsum	2AAV 2BP3 2BRQ 2J3S 2JF1 2K3T 2K7P 2K7Q 2W0P 2WFN 3CNK 3HOC 3HOP 3HOR 3ISW 3RGH 4M9P
ProteinModelPortal	P21333
SMR	P21333
BioGrid	108605
DIP	DIP-1136N
IntAct	P21333
MINT	MINT-118283
STRING	9606.ENSP00000358866
PhosphoSite	P21333
DMDM	116241365
OGP	P21333
MaxQB	P21333
PaxDb	P21333
PRIDE	P21333
Ensembl	ENST00000360319 ENST00000369850 ENST00000422373
GeneID	2316
KEGG	hsa:2316
UCSC	uc004fkk.2 uc010nuu.1
CTD	2316
GeneCards	GC0XM153576
GeneReviews	FLNA
H-InvDB	HIX0017150
HGNC	HGNC:3754
HPA	CAB000356 HPA000368 HPA001115 HPA002925
MIM	300017 300048 300049 300244 300321 300537 304120 305620 309350 311300 314400
neXtProt	NX_P21333
Orphanet	2978 2301 1864 82004 323 1826 2484 90650 90652 98892 88630
PharmGKB	PA28172
eggNOG	COG5069
GeneTree	ENSGT00660000095431
HOGENOM	HOG000044235
HOVERGEN	HBG004163
InParanoid	P21333
KO	K04437
OMA	VQVQDNE
PhylomeDB	P21333
TreeFam	TF313685
Reactome	REACT_20649 REACT_23847
SignaLink	P21333
ChiTaRS	FLNA
EvolutionaryTrace	P21333
GeneWiki	FLNA
GenomeRNAi	2316
NextBio	9405
PMAP-CutDB	P21333
PRO	PR:P21333
Proteomes	UP000005640
Bgee	P21333
CleanEx	HS_FLNA
ExpressionAtlas	P21333
Genevestigator	P21333
GO	GO:0015629 GO:0005884 GO:0097440 GO:0030863 GO:0005737 GO:0005829 GO:0043198 GO:0005576 GO:0070062 GO:0005925 GO:0016020 GO:0031523 GO:0043025 GO:0005634 GO:0048471 GO:0005886 GO:0005802 GO:0051015 GO:0034988 GO:0001948 GO:0044822 GO:0042803 GO:0048365 GO:0017160 GO:0017048 GO:0004871 GO:0031267 GO:0008134 GO:0051764 GO:0031532 GO:0007195 GO:0007596 GO:0034329 GO:0042384 GO:0051220 GO:0045022 GO:0001837 GO:0045184 GO:0042789 GO:0042177 GO:0043433 GO:0030168 GO:0070527 GO:0002576 GO:0043123 GO:0042993 GO:0034394 GO:0050821 GO:0043113 GO:0090307
Gene3D	1.10.418.10 2.60.40.10
InterPro	IPR001589 IPR001715 IPR017868 IPR001298 IPR028559 IPR013783 IPR014756
PANTHER	PTHR11915:SF173
Pfam	PF00307 PF00630
SMART	SM00033 SM00557
SUPFAM	SSF47576 SSF81296
PROSITE	PS00019 PS00020 PS50021 PS50194

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005730	nucleolus	PMID:22307607^[1]	ECO:0000315			C		Figure 1 D&E	complete CACAO 5813
	GO:0016479	negative regulation of transcription from RNA polymerase I promoter	PMID:22307607^[1]	ECO:0000314			P		Figure 2 demonstrates rRNA suppression by FLNA which is needed to segue into the direct assay of Figure 3. Figure 3 shows FLNA association with RNA polymerase I.	complete CACAO 5814
	GO:0030335	positive regulation of cell migration	PMID:23289018^[2]	ECO:0000315			P		Figure 1 and 2 show that inhibition of Filamin-a leads to decreased cell migration.	complete CACAO 7041
	GO:1900026	positive regulation of substrate adhesion-dependent cell spreading	PMID:18177638^[3]	ECO:0000315			P		Figure 3, Knockdown of Filamin-A leads to reduced cell spreading on smooth collagen surface.	complete CACAO 7052
	GO:0043066	negative regulation of apoptotic process	PMID:18177638^[3]	ECO:0000315			P		Figure 5, Filamin-a is required for the survival of cells attached by beta-1 integrins	complete CACAO 7053
	GO:2001046	positive regulation of integrin-mediated signaling pathway	PMID:18177638^[3]	ECO:0000315			P		Figure 7 shows that knockdown of Filamin-a and inhibition of Beta-1 integrin leads to reduced cell spreading, dependent on the inhibition of Beta-1 integrin.	complete CACAO 7054
	GO:0090042	tubulin deacetylation	PMID:26157139^[4]	ECO:0000315			P		Figure 2C-H	complete CACAO 11096
	GO:0008104	protein localization	PMID:26157139^[4]	ECO:0000314			P		Figure 5 shows that Filamin A is required for HDAC5 localization in growth cone	complete CACAO 11165
involved_in	GO:1905000	regulation of membrane repolarization during atrial cardiac muscle cell action potential	GO_REF:0000111	ECO:0000305	curator inference used in manual assertion	GO:1905031	P		Seeded From UniProt	complete
involved_in	GO:1905031	regulation of membrane repolarization during cardiac muscle cell action potential	PMID:24951510^[5]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8BTM8	P	occurs_in:(CL:0002495)	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:24951510^[5]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8BTM8	C		Seeded From UniProt	complete
involved_in	GO:1901381	positive regulation of potassium ion transmembrane transport	PMID:24951510^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0015459	potassium channel regulator activity	PMID:24951510^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q9H2S1)	Seeded From UniProt	complete
involved_in	GO:0072659	protein localization to plasma membrane	PMID:24951510^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	transports_or_maintains_localization_of:(UniProtKB:Q9H2S1)	Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:24951510^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H2S1	F	occurs_in:(UBERON:0000948)	Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25468996^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:25358863^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071526	semaphorin-plexin signaling pathway	PMID:25358863^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:O08665,UniProtKB:Q8BTM8	P		Seeded From UniProt	complete
involved_in	GO:0044319	wound healing, spreading of cells	PMID:16291724^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030334	regulation of cell migration	PMID:16291724^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001664	G protein-coupled receptor binding	PMID:26460884^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25095	F		Seeded From UniProt	complete
enables	GO:0001664	G protein-coupled receptor binding	PMID:26460884^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04201 UniProtKB:P25100 UniProtKB:P30556 UniProtKB:P35462	F		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:22307607^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051020	GTPase binding	PMID:16291724^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P11233	F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:20713593^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P43405	F		Seeded From UniProt	complete
involved_in	GO:2001046	positive regulation of integrin-mediated signaling pathway	PMID:18177638^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:18177638^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900026	positive regulation of substrate adhesion-dependent cell spreading	PMID:18177638^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016479	negative regulation of transcription by RNA polymerase I	PMID:22307607^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21914078^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070527	platelet aggregation	PMID:23382103^[12]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005911	cell-cell junction	PMID:16291724^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0031941	filamentous actin	PMID:25358863^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051764	actin crosslink formation	PMID:10051605^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051220	cytoplasmic sequestering of protein	PMID:17536008^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:4044584^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:3138234^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:2391361^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:18322202^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0048365	Rac GTPase binding	PMID:10051605^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045184	establishment of protein localization	PMID:18322202^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043113	receptor clustering	PMID:10692483^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:2391361^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042177	negative regulation of protein catabolic process	PMID:18322202^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0034988	Fc-gamma receptor I complex binding	PMID:1833070^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034394	protein localization to cell surface	PMID:18322202^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031532	actin cytoskeleton reorganization	PMID:10051605^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031267	small GTPase binding	PMID:10051605^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0017160	Ral GTPase binding	PMID:10051605^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0017048	Rho GTPase binding	PMID:10051605^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:2391361^[22]	ECO:0000305	curator inference used in manual assertion	GO:0051015	C		Seeded From UniProt	complete
involved_in	GO:0007195	adenylate cyclase-inhibiting dopamine receptor signaling pathway	PMID:10692483^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:18322202^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21362503^[26]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002367)	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[27]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[28]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043433	negative regulation of DNA-binding transcription factor activity	PMID:15684392^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:12761501^[30]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042307	positive regulation of protein import into nucleus	PMID:15684392^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P40424-1)	Seeded From UniProt	complete
involved_in	GO:0060271	cilium assembly	PMID:22121117^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:15684392^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12948	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15684392^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15684392^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090307	mitotic spindle assembly	PMID:18548008^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031523	Myb complex	PMID:18548008^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2001224	positive regulation of neuron migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
involved_in	GO:2000179	positive regulation of neural precursor cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
involved_in	GO:1902396	protein localization to bicellular tight junction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0097440	apical dendrite	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
involved_in	GO:0097368	establishment of Sertoli cell barrier	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	F		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	F		Seeded From UniProt	complete
part_of	GO:0043198	dendritic shaft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
involved_in	GO:0042789	mRNA transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
involved_in	GO:0032233	positive regulation of actin filament bundle assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
enables	GO:0031852	mu-type opioid receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	F		Seeded From UniProt	complete
part_of	GO:0030863	cortical cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
involved_in	GO:0021987	cerebral cortex development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
involved_in	GO:0021943	formation of radial glial scaffolds	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	P		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0005938	cell cortex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0005884	actin filament	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C0JPT7 ensembl:ENSRNOP00000070703	C		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028559	F		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	Reactome:R-HSA-8983711	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034329	cell junction assembly	Reactome:R-HSA-446728	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030168	platelet activation	Reactome:R-HSA-76002	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8985123 Reactome:R-HSA-5669250 Reactome:R-HSA-5669240 Reactome:R-HSA-482772 Reactome:R-HSA-430347 Reactome:R-HSA-430096	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-482772	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002576	platelet degranulation	Reactome:R-HSA-114608	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030030	cell projection organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0970	P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0009	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005938	cell cortex	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0138	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Deng, W et al. (2012) Cytoskeletal protein filamin A is a nucleolar protein that suppresses ribosomal RNA gene transcription. Proc. Natl. Acad. Sci. U.S.A. 109 1524-9 PubMed GONUTS page
↑ Jiang, X et al. (2013) Inhibition of filamin-A reduces cancer metastatic potential. Int. J. Biol. Sci. 9 67-77 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Kim, H et al. (2008) Filamin A regulates cell spreading and survival via beta1 integrins. Exp. Cell Res. 314 834-46 PubMed GONUTS page
↑ ^4.0 ^4.1 Cho, Y et al. (2015) Filamin A is required in injured axons for HDAC5 activity and axon regeneration. J. Biol. Chem. 290 22759-70 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 Rafizadeh, S et al. (2014) Functional interaction with filamin A and intracellular Ca2+ enhance the surface membrane expression of a small-conductance Ca2+-activated K+ (SK2) channel. Proc. Natl. Acad. Sci. U.S.A. 111 9989-94 PubMed GONUTS page
↑ ^6.0 ^6.1 Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Nakamura, F et al. (2014) Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling. Nat Commun 5 5325 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Klaile, E et al. (2005) CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration. J. Cell. Sci. 118 5513-24 PubMed GONUTS page
↑ ^9.0 ^9.1 Tirupula, KC et al. (2015) G protein-coupled receptors directly bind filamin A with high affinity and promote filamin phosphorylation. Biochemistry 54 6673-83 PubMed GONUTS page
↑ Falet, H et al. (2010) A novel interaction between FlnA and Syk regulates platelet ITAM-mediated receptor signaling and function. J. Exp. Med. 207 1967-79 PubMed GONUTS page
↑ Ghosh, S et al. (2011) Association of filamin A and vimentin with hepatitis C virus proteins in infected human hepatocytes. J. Viral Hepat. 18 e568-77 PubMed GONUTS page
↑ Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^17.0 ^17.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Ohta, Y et al. (1999) The small GTPase RalA targets filamin to induce filopodia. Proc. Natl. Acad. Sci. U.S.A. 96 2122-8 PubMed GONUTS page
↑ Cho, EY et al. (2007) Roles of protein kinase C and actin-binding protein 280 in the regulation of intracellular trafficking of dopamine D3 receptor. Mol. Endocrinol. 21 2242-54 PubMed GONUTS page
↑ Fox, JE (1985) Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membranes. J. Biol. Chem. 260 11970-7 PubMed GONUTS page
↑ Ezzell, RM et al. (1988) Localization of the domain of actin-binding protein that binds to membrane glycoprotein Ib and actin in human platelets. J. Biol. Chem. 263 13303-9 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Gorlin, JB et al. (1990) Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J. Cell Biol. 111 1089-105 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 Beekman, JM et al. (2008) Filamin A stabilizes Fc gamma RI surface expression and prevents its lysosomal routing. J. Immunol. 180 3938-45 PubMed GONUTS page
↑ ^24.0 ^24.1 Li, M et al. (2000) Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280). Mol. Pharmacol. 57 446-52 PubMed GONUTS page
↑ Ohta, Y et al. (1991) Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (Fc gamma RI). Cell 67 275-82 PubMed GONUTS page
↑ Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 Berry, FB et al. (2005) FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin A-mediated manner. Mol. Cell. Biol. 25 1415-24 PubMed GONUTS page
↑ Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page
↑ Adams, M et al. (2012) A meckelin-filamin A interaction mediates ciliogenesis. Hum. Mol. Genet. 21 1272-86 PubMed GONUTS page
↑ ^32.0 ^32.1 Yamauchi, T et al. (2008) A B-Myb complex containing clathrin and filamin is required for mitotic spindle function. EMBO J. 27 1852-62 PubMed GONUTS page

[PMID:22307607-1] 1.0 ^1.1 ^1.2 ^1.3 Deng, W et al. (2012) Cytoskeletal protein filamin A is a nucleolar protein that suppresses ribosomal RNA gene transcription. Proc. Natl. Acad. Sci. U.S.A. 109 1524-9 PubMed GONUTS page

[PMID:23289018-2] Jiang, X et al. (2013) Inhibition of filamin-A reduces cancer metastatic potential. Int. J. Biol. Sci. 9 67-77 PubMed GONUTS page

[PMID:18177638-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Kim, H et al. (2008) Filamin A regulates cell spreading and survival via beta1 integrins. Exp. Cell Res. 314 834-46 PubMed GONUTS page

[PMID:26157139-4] 4.0 ^4.1 Cho, Y et al. (2015) Filamin A is required in injured axons for HDAC5 activity and axon regeneration. J. Biol. Chem. 290 22759-70 PubMed GONUTS page

[PMID:24951510-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 Rafizadeh, S et al. (2014) Functional interaction with filamin A and intracellular Ca2+ enhance the surface membrane expression of a small-conductance Ca2+-activated K+ (SK2) channel. Proc. Natl. Acad. Sci. U.S.A. 111 9989-94 PubMed GONUTS page

[PMID:25468996-6] 6.0 ^6.1 Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:25358863-7] 7.0 ^7.1 ^7.2 Nakamura, F et al. (2014) Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling. Nat Commun 5 5325 PubMed GONUTS page

[PMID:16291724-8] 8.0 ^8.1 ^8.2 ^8.3 Klaile, E et al. (2005) CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration. J. Cell. Sci. 118 5513-24 PubMed GONUTS page

[PMID:26460884-9] 9.0 ^9.1 Tirupula, KC et al. (2015) G protein-coupled receptors directly bind filamin A with high affinity and promote filamin phosphorylation. Biochemistry 54 6673-83 PubMed GONUTS page

[PMID:20713593-10] Falet, H et al. (2010) A novel interaction between FlnA and Syk regulates platelet ITAM-mediated receptor signaling and function. J. Exp. Med. 207 1967-79 PubMed GONUTS page

[PMID:21914078-11] Ghosh, S et al. (2011) Association of filamin A and vimentin with hepatitis C virus proteins in infected human hepatocytes. J. Viral Hepat. 18 e568-77 PubMed GONUTS page

[PMID:23382103-12] Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page

[PMID:21423176-13] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:23533145-14] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19946888-15] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19056867-16] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-17] 17.0 ^17.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:10051605-18] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Ohta, Y et al. (1999) The small GTPase RalA targets filamin to induce filopodia. Proc. Natl. Acad. Sci. U.S.A. 96 2122-8 PubMed GONUTS page

[PMID:17536008-19] Cho, EY et al. (2007) Roles of protein kinase C and actin-binding protein 280 in the regulation of intracellular trafficking of dopamine D3 receptor. Mol. Endocrinol. 21 2242-54 PubMed GONUTS page

[PMID:4044584-20] Fox, JE (1985) Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membranes. J. Biol. Chem. 260 11970-7 PubMed GONUTS page

[PMID:3138234-21] Ezzell, RM et al. (1988) Localization of the domain of actin-binding protein that binds to membrane glycoprotein Ib and actin in human platelets. J. Biol. Chem. 263 13303-9 PubMed GONUTS page

[PMID:2391361-22] 22.0 ^22.1 ^22.2 Gorlin, JB et al. (1990) Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J. Cell Biol. 111 1089-105 PubMed GONUTS page

[PMID:18322202-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 Beekman, JM et al. (2008) Filamin A stabilizes Fc gamma RI surface expression and prevents its lysosomal routing. J. Immunol. 180 3938-45 PubMed GONUTS page

[PMID:10692483-24] 24.0 ^24.1 Li, M et al. (2000) Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280). Mol. Pharmacol. 57 446-52 PubMed GONUTS page

[PMID:1833070-25] Ohta, Y et al. (1991) Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (Fc gamma RI). Cell 67 275-82 PubMed GONUTS page

[PMID:21362503-26] Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page

[PMID:22658674-27] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:22681889-28] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:15684392-29] 29.0 ^29.1 ^29.2 ^29.3 ^29.4 Berry, FB et al. (2005) FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin A-mediated manner. Mol. Cell. Biol. 25 1415-24 PubMed GONUTS page

[PMID:12761501-30] Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page

[PMID:22121117-31] Adams, M et al. (2012) A meckelin-filamin A interaction mediates ciliogenesis. Hum. Mol. Genet. 21 1272-86 PubMed GONUTS page

[PMID:18548008-32] 32.0 ^32.1 Yamauchi, T et al. (2008) A B-Myb complex containing clathrin and filamin is required for mitotic spindle function. EMBO J. 27 1852-62 PubMed GONUTS page

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HUMAN:FLNA

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